Crystalline farnesyl protein transferase compositions and methods for use

ABSTRACT

The present invention relates to crystalline compositions comprising farnesyl protein transferase-like polypeptides in complex with substrates and inhibitors. Also disclosed are crystallization conditions for these compositions and their use for structural determination of FPT:FPP/FPP analog: peptide/inhibitor complexes.

This application claims priority from U.S. Provisional Application Serial No. 60/098,331, filed Aug. 28, 1998, which is incorporated entirely herein.

TECHNICAL FIELD OF INVENTION

The present invention relates to crystalline farnesyl protein transferase (FPT) and FPT in complex with substrates or inhibitors. This invention also relates to methods of using the structure coordinates of FPT to solve the structure of similar or homologous proteins or protein substrate or inhibitor complexes.

BACKGROUND OF THE INVENTION

The biological significance of the Ras oncogene, and the role of both Ras and the enzyme known as farnesyl protein transferase (“FPT”) in the conversion of normal cells to cancer cells, are described in PCT International Publication Nos. WO95/00497 and WO95/10516. To undergo transforming potential, the precursor of the Ras oncoprotein must undergo farnesylation of the cysteine residue located in a carboxyl-terminal tetrapeptide. Farnesyl protein transferase catalyzes this modification. Inhibitors of this enzyme have therefore been suggested as anticancer agents for tumors in which RAS contributes to transformation.

Drug discovery efforts directed toward FPT inhibitors have been hampered by the lack of adequate structural information about FPT and its complex with substrates and inhibitors. The structure of FPT was first determined at Duke University using a crystalline form where the active site was blocked by the carboxy terminus of an adjacent molecule in the crystalline lattice. Beese et al., 1997, Science 275:1800-1804. These crystals are not suited for drug discovery because, as reported therein, the active site is blocked by part of the crystal lattice. Another crystalline form of FPT was also reported in Dunten et al., 1998, Biochemistry 37(22):7907-7912. These crystals grow at pH 4.4 and are reported to only diffract to 2.8 Å resolution. However, the authors point out that there are no substrates or peptide inhibitors bound due to the low pH of the crystallization. Thus these crystals are not suitable for structure-based drug design.

Structural information from FPT crystalline complexes would provide valuable information in discovery of FPT inhibitors. This information could be used to design more potent, selective and metabolically stable FPT inhibitors for use as drugs against cancer.

SUMMARY OF THE INVENTION

Applicants have solved this problem by providing crystalline compositions comprising a farnesyl protein transferase (FPT) complexed with its natural substrates and with molecules that mimic its natural substrates. The invention also provides the structure coordinates of these complexes. Further provided are methods for soaking these crystalline complexes in the presence of an inhibitor, thereby efficiently forming new crystalline enzyme: inhibitor complexes.

The invention also provides a method for determining at least a portion of the three-dimensional structure of molecules or molecular complexes which contain at least some structurally similar features to an FPT: substrate or FPT: inhibitor complex.

BRIEF DESCRIPTION OF THE FIGURES

FIG. 1 depicts stereo ribbon diagrams of an FPT:αHFP:Ac-CVIM-COOH complex. The view is into the active site cavity of the enzyme.

FIG. 2 shows a diagram of a system used to carry out the instructions encoded by the storage medium of FIGS. 3 and 4.

FIG. 3 shows a cross section of a magnetic storage medium.

FIG. 4 shows a cross section of a optically-readable data storage medium.

DETAILED DESCRIPTION OF THE INVENTION

FPT-mediated prenylation of Ras involves formation of a ternary complex comprising farnesyl protein transferase (FPT), farnesyl diphosphate (FPP) and Ras (FPT:FPP:Ras), followed by transfer of the 15-carbon isoprenoid from FPP to a cysteine sidechain of Ras. The cysteine residue is part of a conserved carboxyl terminal Ca₁a₂X (SEQ ID No: 4) sequence where X is a serine residue in H-Ras and methionine in N-Ras, K-Ras 4a, and K-Ras 4b isoforms.

Applicants have discovered crystalline forms of farnesyl protein transferase (FPT) suited for structure-based drug design. Provided herein are two basic crystal forms—wherein an FPT-like polypeptide is complexed with FPP and an inhibitor, and wherein an FPT-like polypeptide is complexed with molecules that mimic the natural substrates. (These complexes are referred to throughout as FPT:FPP/FPP analog:Peptide/Inhibitor complexes.)

The FPT-like polypeptide portion of the complex is any polypeptide that has the activity of naturally occurring FPT (Reiss et al, 1990, Cell 62:81-88), particularly the ability to cause farnesylation of the cysteine residue located in a carboxyl-terminal tetrapeptide of the precursor of the Ras oncoprotein. The terms “FPT” and “FPT-like polypeptide” are used interchangeably herein and include FPT and polypeptides that differ from FPT by having amino acid deletions, substitutions, and additions, but which retain the activity of FPT.

In one embodiment, FPT is complexed with farnesyl diphosphate (FPP) and an inhibitor. These crystals diffract to at least 2.2 Å resolution. At this resolution, most atoms of the FPT:FPP:inhibitor complex can be visualized using x-ray crystallographic methods.

In another embodiment, the pre-formed crystals of FPT are grown by first complexing FPT with molecules that mimic the natural substrates. FPT is complexed with an FPP analog and a tetrapeptide substrate based on the carboxy terminus of Ras referred to herein as a Ca₁a₂X (SEQ ID No: 4) peptide. Preferably, the FPP analog used is α-hydroxyphosphonic acid (αHFP) (Calbiochem-Novabiochem Corp.), and the Ca₁a₂X (SEQ ID No: 4) peptide is N-acetyl-Cys-Val-Ile-Met-COOH (CVIM) (SEQ ID No: 1) (SynPep Inc.). These crystals diffract to 2.4 Å resolution. At this resolution, most atoms of the complex can be visualized using x-ray crystallographic methods.

Those skilled in the art will understand, of course, that other FPP analogs and other Ca₁a₂X (SEQ ID No: 4) peptides may be used in these complexes. For example, methylene-farnesyl diphosphate [Davisson et al, 1986, J. Org. Chem. 51:4768-4779] can also be used in place of αHFP as an FPP analog, however any analog of FPP could be used. Likewise, many other Ca₁a₂X (SEQ ID No: 4) peptides may be used. In preferred embodiments, X is serine, methionine, cysteine, alanine or glutamine. See Reiss et al, 1991, PNAS 88:732-36. A variety of both natural and unnatural amino acids can be accommodated at the a₁ position without loss of activity. Peptides having small apolar residues at a₂ are also good substrates, while those with aromatic sidechains at this position competitively inhibit binding of peptide substrates. Goldstein et al., J. Biol Chem 266:15575-15578. In more preferred embodiments, the Ca₁a₂X (SEQ ID No: 4).

The pre-formed FPT:FPP analog: peptide crystals of this invention can be soaked in the presence of an inhibitor, thereby forming new protein/compound complexes and obviating the need to crystallize each individual protein/compound complex. Crystalline complexes of FPT with FPP and an inhibitor can also be soaked in the presence of another inhibitor so that the original inhibitor is displaced and a new crystalline FPT:FPP:inhibitor complex is formed. The ability to form FPT:FPP:inhibitor complexes in the crystalline state allows very rapid turnaround of structural information.

According to one embodiment of the invention, an FPT:αHFP:CVIM complex is crystallized from a well-defined solution. A solution for stabilizing the crystals (artificial mother liquor) has been discovered. To obtain the structure of FPT inhibitors complexed with FPT, the crystals of FPT:αHFP:CVIM are soaked in solutions of artificial mother liquor containing inhibitor and farnesyl diphosphate (FPP). The crystalline nature of FPT is retained during this procedure, only the molecules bound to the active site are altered.

The present invention provides the three-dimensional structure of (1) an FPT:αHFP:CVIM peptide complex at 2.4 Å resolution, (2) an FPT:FPP:SCH66381 complex at 2.2 Å resolution, (3) an FPT:FPP:SCH66701 complex at 2.9 Å resolution, and (4) an FPT:FPP:SCH69132 complex at 2.5 Å resolution. Importantly, the crystalline structures of the present invention provide information about the shape and structure of the FPT active site containing both an isoprenoid and a peptide or inhibitor.

The three-dimensional structures of three FPT complexes of this invention are defined by a set of structure coordinates as set forth in FIGS. 2-5. The term “structure coordinates” refers to Cartesian coordinates derived from mathematical equations related to the patterns obtained on diffraction of a monochromatic beam of X-rays by the atoms (scattering centers) of FPT:FPP/FPP analog:Peptide/Inhibitor complexes in crystal form. The diffraction data are used to calculate an electron density map of the repeating unit of the crystal. The electron density maps are then used to establish the positions of the individual atoms of the FPT:FPP/FPP analog: Peptide/Inhibitor complexes.

Those of skill in the art will understand that a set of structure coordinates for an enzyme or an enzyme-complex or a portion thereof, is a relative set of points that define a shape in three dimensions. Thus, it is possible that an entirely different set of coordinates could define a similar or identical shape. Moreover, slight variations in the individual coordinates will have little effect on overall shape.

The variations in coordinates discussed above may be generated because of mathematical manipulations of the structure coordinates. For example, the structure coordinates set forth in Tables 2-5 could be manipulated by crystallographic permutations of the structure coordinates, fractionalization of the structure coordinates, rotation of the structure coordinates, integer additions or subtractions to sets of the structure coordinates, inversion of the structure coordinates or any combination of the above.

Alternatively, modifications in the crystal structure due to mutations, additions, substitutions, and/or deletions of amino acids, or other changes in any of the components that make up the crystal could also account for variations in structure coordinates. If such variations are within an acceptable standard error as compared to the original coordinates, the resulting three-dimensional shape is considered to be the same.

Various computational analyses are therefore necessary to determine whether a molecule or molecular complex or a portion thereof is sufficiently similar to all or parts of the FPT enzyme or enzyme complex as described above as to be considered the same. Such analyses may be performed using automated or manual tools in current software applications, such as those sold by Molecular Simulations Incorporated, and referred to as INSIGHT or QUANTA.

The Molecular Similarity application,(Molecular Simulations Incorporated) permits comparisons between different structures, different conformations of the same structure, and different parts of the same structure. The procedure used in Molecular Similarity to compare structures is divided into four steps: 1) load the structures to be compared; 2) define the atom equivalencies in these structures; 3) perform a fitting operation; and 4) analyze the results.

Each structure is identified by a name. One structure is identified as the target (i.e., the fixed structure); all remaining structures are working structures (i.e., moving structures). Since atom equivalency within QUANTA is defined by user input, for the purpose of this invention we will define equivalent atoms as protein backbone atoms (N, Ca, C and O) for all conserved residues between the two structures being compared.

When a rigid fitting method is used, the working structure is translated and rotated to obtain an optimum fit with the target structure. The fitting operation uses an algorithm that computes the optimum translation and rotation to be applied to the moving structure, such that the root mean square difference of the fit over the specified pairs of equivalent atom is an absolute minimum. This number, given in angstroms, is reported by QUANTA.

For the purpose of this invention, any molecule or molecular complex that has a root mean square deviation of conserved residue backbone atoms (N, Ca, C, O) of less than 3 Å when superimposed on the relevant backbone atoms described by structure coordinates listed in any one of Tables 2-5 are considered identical. More preferably, the root mean square deviation is less than 1.0 Å.

The term “root mean square deviation” means the square root of the arithmetic mean of the squares of the deviations from the mean. It is a way to express the deviation or variation from a trend or object. For purposes of this invention, the “root mean square deviation” defines the variation in the backbone of a protein or protein complex from the relevant portion of the backbone of the FPT-like polypeptide portion of the complex as defined by the structure coordinates described herein.

Once the structure coordinates of a protein crystal have been determined they are useful in solving the structures of other crystals.

Thus, in accordance with the present invention, the structure coordinates of an FPT:FPP/FPP analog: peptide/Inhibitor complex and portions thereof are stored in a machine-readable storage medium. Such data may be used for a variety of purposes, such as drug discovery and X-ray crystallographic analysis of protein crystals.

Accordingly, in one embodiment of this invention is provided a machine-readable data storage medium comprising a data storage material encoded with the structure coordinates set forth in Table 2, 3, 4 or 5.

FIG. 2 demonstrates one version of these embodiments. System 10 includes a computer 11 comprising a central processing unit (“CPU”) 20, a working memory 22 which may be, e.g. RAM (random-access memory) or “core” memory, mass storage memory 24 (such as one or more disk drives or CD-ROM drives), one or more cathode-ray tube (“CRT”) display terminals 26, one or more keyboards 28, one or more input lines 30, and one or more output lines 40, all of which are interconnected by a conventional bi-directional system bus 50.

Input hardware 36, coupled to computer 11 by input lines 30, may be implemented in a variety of ways. Machine-readable data of this invention may be inputted via the use of a modem or modems 32 connected by a telephone line or dedicated data line 34. Alternatively or additionally, the input hardware 36 may comprise CD-ROM drives or disk drives 24. In conjunction with display terminal 26, keyboard 28 may also be used as an input device.

Output hardware 46, coupled to computer 11 by output lines 40, may similarly be implemented by conventional devices. By way of example, output hardware 46 may include CRT display terminal 26 for displaying a graphical representation of a binding pocket of this invention using a program such as INSIGHT as described herein. Output hardware might also include a printer 42, so that hard copy output may be produced, or a disk drive 24, to store system output for later use.

In operation, CPU 20 coordinates the use of the various input and output devices 36, 46, coordinates data accesses from mass storage 24 and accesses to and from working memory 22, and determines the sequence of data processing steps. A number of programs may be used to process the machine-readable data of this invention. Such programs are discussed in reference to the computational methods of drug discovery as described herein. Specific references to components of hardware system 10 are included as appropriate throughout the following description of the data storage medium.

FIG. 3 shows a cross section of a magnetic data storage medium 100 which can be encoded with a machine-readable data that can be carried out by a system such as system 10 of FIG. 2. Medium 100 can be a conventional floppy diskette or hard disk, having a suitable substrate 101, which may be conventional, and a suitable coating 102, which may be conventional, on one or both sides, containing magnetic domains (not visible) whose polarity or orientation can be altered magnetically. Medium 100 may also have an opening (not shown) for receiving the spindle of a disk drive or other data storage device 24.

The magnetic domains of coating 102 of medium 100 are polarized or oriented so as to encode in manner which may be conventional, machine readable data such as that described herein, for execution by a system such as system 10 of FIG. 2.

FIG. 4 shows a cross section of an optically-readable data storage medium 110 which also can be encoded with such a machine-readable data, or set of instructions, which can be carried out by a system such as system 10 of FIG. 2. Medium 110 can be a conventional compact disk read only memory (CD-ROM) or a rewritable medium such as a magneto-optical disk which is optically readable and magneto-optically writable. Medium 100 preferably has a suitable coating 112, which may be conventional, usually of one side of substrate 111.

In the case of CD-ROM, as is well known, coating 112 is reflective and is impressed with a plurality of pits 113 to encode the machine-readable data. The arrangement of pits is read by reflecting laser light off the surface of coating 112. A protective coating 114, which preferably is substantially transparent, is provided on top of coating 112.

In the case of a magneto-optical disk, as is well known, coating 112 has no pits 113, but has a plurality of magnetic domains whose polarity or orientation can be changed magnetically when heated above a certain temperature, as by a laser (not shown). The orientation of the domains can be read by measuring the polarization of laser light reflected from coating 112. The arrangement of the domains encodes the data as described above.

The present invention permits the use of structure-based or rational drug design techniques to design, select, and synthesize chemical entities, including inhibitory compounds that are capable of binding to the active site of FPT, or any portion thereof.

One particularly useful drug design technique enabled by this invention is iterative drug design. Iterative drug design is a method for optimizing associations between a protein and a compound by determining and evaluating the three-dimensional structures of successive sets of FPT:FPP or FPP analog:Peptide or Inhibitor complexes.

Those of skill in the art will realize that association of natural ligands or substrates with the binding pockets of their corresponding receptors or enzymes is the basis of many biological mechanisms of action. The term “binding pocket,” as used herein, refers to a region of a molecule or molecular complex, that, as a result of its shape, favorably associates with another chemical entity or compound. Similarly, many drugs exert their biological effects through association with the binding pockets of receptors and enzymes. Such associations may occur with all or any parts of the binding pockets. An understanding of such associations will help lead to the design of drugs having more favorable associations with their target receptor or enzyme, and thus, improved biological effects. Therefore, this information is valuable in designing potential ligands or inhibitors of receptors or enzymes, such as inhibitors of FPT.

The term “associating with” refers to a condition of proximity between chemical entities or compounds, or portions thereof. The association may be non-covalent—wherein the juxtaposition is energetically favored by exclusively or a combination of hydrogen bonding or van der Waals and/or electrostatic interactions—or it may be covalent.

In iterative drug design, crystals of a series of protein/compound complexes are obtained and then the three-dimensional structure of each complex is solved. Such an approach provides insight into the association between the proteins and compounds of each complex. This is accomplished by selecting compounds with inhibitory activity, obtaining crystals of this new protein/compound complex, solving the three-dimensional structure of the complex, and comparing the associations between the new protein/compound complex and previously solved protein/compound complexes. By observing how changes in the compound affected the protein/compound associations, these associations may be optimized.

In some cases, iterative drug design is carried out by forming successive protein-compound complexes and then crystallizing each new complex. Alternatively, a pre-formed protein crystal is soaked in the presence of an inhibitor, thereby forming a protein/compound complex and obviating the need to crystallize each individual protein/compound complex. Advantageously, the FPT:FPP/FPP analog:Peptide/Inhibitor complex crystals, and in particular the FPT:αHFP:CVIM crystals, provided by this invention may be soaked in the presence of a compound or compounds, to provide FPT:FPP:inhibitor crystal complexes.

As used herein, the term “soaked” refers to a process in which the crystal is transferred to a solution containing the compound of interest.

The structure coordinates set forth in Tables 2-5 can also be used to aid in obtaining structural information about another crystallized molecule or molecular complex. This may be achieved by any of a number of well-known techniques, including molecular replacement.

The structure coordinates set forth in Tables 2-5 can also be used for determining at least a portion of the three-dimensional structure of molecules or molecular complexes which contain at least some structurally similar features to FPT. In particular, structural information about another crystallized molecule or molecular complex may be obtained. This may be achieved by any of a number of well-known techniques, including molecular replacement.

Therefore, in another embodiment this invention provides a method of utilizing molecular replacement to obtain structural information about a crystallized molecule or molecular complex whose structure is unknown comprising the steps of:

a) generating an X-ray diffraction pattern from said crystallized molecule or molecular complex; and

b) applying at least a portion of the structure coordinates set forth in any one of Tables 2-5 to the X-ray diffraction pattern to generate a three-dimensional electron density map of the molecule or molecular complex whose structure is unknown.

By using molecular replacement, all or part of the structure coordinates of the FPT:FPP/FPP analog:Peptide/Inhibitor complexes provided by this invention (and set forth in Tables) can be used to determine the structure of a crystallized molecule or molecular complex whose structure is unknown more quickly and efficiently than attempting to determine such information ab initio or by isomorphous replacement methods.

Molecular replacement provides an accurate estimation of the phases for an unknown structure. Phases are a factor in equations used to solve crystal structures that can not be determined directly. Obtaining accurate values for the phases, by methods other than molecular replacement, is a time-consuming process that involves iterative cycles of approximations and refinements and greatly slows the solution of crystal structures. However, when the crystal structure of a protein containing at least a homologous portion has been solved, the phases from the known structure provide a satisfactory estimate of the phases for the unknown structure.

Thus, this method involves generating a preliminary model of a molecule or molecular complex whose structure coordinates are unknown, by orienting and positioning the relevant portion of the complex according to any one of Tables 2-5 within the unit cell of the crystal of the unknown molecule or molecular complex so as best to account for the observed X-ray diffraction pattern of the crystal of the molecule or molecular complex whose structure is unknown. Phases can then be calculated from this model and combined with the observed X-ray diffraction pattern amplitudes to generate an electron density map of the structure whose coordinates are unknown. This, in turn, can be subjected to any well-known model building and structure refinement techniques to provide a final, accurate structure of the unknown crystallized molecule or molecular complex (E. Lattman, “Use of the Rotation and Translation Functions,” in Meth. Enzymol., 115, pp. 55-77 (1985); M. G. Rossmann, ed., “The Molecular Replacement Method,” Int. Sci. Rev. Ser., No. 13, Gordon & Breach, New York (1972).

The structure of any portion of any crystallized molecule or molecular complex that is sufficiently homologous to any portion of the FPT:FPP/FPP analog:Peptide/Inhibitor complex can be solved by this method.

In a preferred embodiment, the method of molecular replacement is utilized to obtain structural information about a molecule or molecular complex, wherein the complex comprises an FPT:FPP/FPP analog:Peptide/Inhibitor complex.

The structure coordinates provided by this invention are particularly useful to solve the structure of crystals of FPT:FPP/FPP analog:Peptide/Inhibitor complexes, particularly FPT:FPP, co-complexed with a variety of chemical entities. This approach enables the determination of the optimal sites for interaction between chemical entities, including interaction of candidate FPT inhibitors with FPT or the FPT:FPP complex. For example, high resolution X-ray diffraction data collected from crystals exposed to different types of solvent allows the determination of where each type of solvent molecule resides. Small molecules that bind tightly to those sites can then be designed and synthesized and tested for their FPT inhibition activity.

All of the complexes referred to above may be studied using well-known X-ray diffraction techniques and may be refined versus 1.5-3 Å resolution X-ray data to an R value of about 0.25 or less using computer software, such as XPLOR [Yale University, ©1992; see, e.g., Blundell & Johnson, supra; Meth. Enzymol., vol. 114 and 115, H. W. Wyckoff et al., eds., Academic Press (1985)]. This information may thus be used to optimize known FPT inhibitors, and more importantly, to design new FPT inhibitors.

In order that this invention be more fully understood, the following examples are set forth. These examples are for the illustrative purposes only and are not to be construed as limiting the scope of this invention in any way.

EXAMPLE 1 Expression and Purification of FPT in Sf9 Cells For Analog Complexes

Preparation of Expression Constructs

Rat FPT α and β subunit cDNAs in pUC13 were obtained from ATCC (ATCC clone numbers 63134 and 63127 respectively). The rat α subunit cDNA was excised from pUC13 with Eco RI (5′) and Hind III (3′) and ligated downstream of the polyhedron promoter in p2Bac (Invitrogen) cut with Eco RI and Hind III to produce pRatA-2B. The ATG start codon in the Nco I site upstream of the rat α subunit in pRatA-2B was removed by cutting with Nco I, removing the single stranded ends with mung bean nuclease, and religating the blunt ends together to produce pRatAN-2B. The rat β subunit was excised from pUC13 with Xma I (5′) and Nhe I (3′) and ligated downstream of the P10 promoter in pRatAN-2B cut with Xma I (5′) and Xba I (3′) to produce pRABN-Bac.

pRABN-Bac was co-transfected with Baculovirus Gold DNA (Pharmingen) into Sf9 cells following the manufacturer's protocol. Recombinant baculoviruses were plaque purified and individual clones were tested for expression of FPT activity by SPA (Amersham) and for protein expression by Western blot (Santa Cruz anti-rat FPT antibodies). The highest expressing virus was amplified to high titre (>10⁹/ml) in Sf9 cells (infecting at MOI <0.1 to retard amplification of defective viruses).

Expression and Purification of Rat FPT from Sf9 Cells

Protein purification was conducted at 4° C. At each stage of the purification eluted proteins were detected by absorbance at 280 nm and active enzyme fractions were assayed by the SPA assay as described below. Western blotting during protein purification was carried out according to a standard protocol using a BCIP/NBT kit (Kirkegaard & Perry Laboratories, Gaitherburg, Md.) with an anti-α subunit polyclonal antibody raised against two peptide sequences of FPT α subunit and an anti-β subunit polyclonal antibody obtained from Santa Cruz Biotechnology (Santa Cruz, Calif.). The molecular weight of FPT was determined by MALDI mass spectroscopy with sinapinic acid as the matrix on a Voyager DE TOF mass spectrometer (PerSeptive Biosystem, Framingham, Mass.). FPT concentrations were determined either by the method of Bradford using a Bio-Rad assay kit with bovine serum albumin (BSA) as a standard or using UV absorption at 280 nm with a molar extinction coefficient of 1.53×10⁵ M⁻¹ cm⁻¹.

Ten liters of Sf9 cells were grown at 27° C. to a cell density of 4.0×10⁶ cells/ml in SF 900II Media (GibcoBRL). Bacculovirus construct RABN-Bac containing the rat FPT gene was added at a multiplicity of infection (MOI) of 2:1. This culture was incubated until the cell viability reached 60-70% (approximately 3 days). Cells were harvested by centrifugation for 20 min at 4° C. and produced ˜100 g of a wet cell pellet. The cell pellet was resuspended in 300 ml homogenization buffer containing 50 mM Tris-HCl, pH 7.5, 1 μg/ml E-64, 2 μg/ml aprotinin, 0.7 μg/ml pepstatin, 0.1 mM leupeptin, 1 mM Pefabloc® SC, 1 mM EDTA, 1 mM EGTA and 1 mM DTT (inhibitors from Boehringer Mannheim, DTT from Calbiochem). The resuspended cells were disrupted by pressure using a microfluidizer (Microfluidics Corporation, Newton, Mass.). Cell debris was removed by ultracentrifugation at 100,000 g for 1 hr. The supernatant, containing 1-3% FPT, was adjusted to 2 mM DTT and pH 7.7 then loaded onto a Fast Flow Q-Sepharose column (5×10 cm, Pharmacia) equilibrated in 20 mM Tris, 0.15 M NaCl, 10 μM ZnCl₂, 2 mM DTT, pH 7.7. The column was washed with the equilibration buffer, followed by a salt gradient of 0.15 M to 0.5 M NaCl. FPT activity eluted at about 300 mM NaCl and was ˜10% pure. The active fractions were adjusted to 0.75 M NaCl using a 5 M NaCl stock solution. This sample was loaded onto a Phenyl Sepharose CL-4B column (Pharmacia), washed with the same starting buffer and the protein was eluted using a 0.75 M-0 M NaCl gradient. The protein eluted at the end of the gradient ˜0 M NaCl and was ˜50-70% pure. The pooled rat FPT fractions were adjusted to 0.1 M NaCl and loaded onto a Mono Q HR10/10 column (Pharmacia), washed with the same buffer and eluted with a gradient of 0.1-0.5 M NaCl. The active fractions eluted ˜0.3 M NaCl and were 60-80% pure. The active fractions were pooled and the buffer was adjusted to 0.75 M NaCl, 20 mM Tris, 10 μM ZnCl₂, 1 mM DTT, pH 7.7. This sample was loaded onto a Phenyl Superose HR 10/10 column (Pharmacia), washed with the starting buffer and sample eluted using a 0.75-0 M NaCl gradient. FPT fractions (eluting ˜0 M NaCl) that were >95% pure were pooled and dialyzed into a storage buffer consisting of 20 mM Tris-HCl, 20 mM KCl, 10 μM ZnCl₂, 1 mM DTT, pH 7.7. The resulting protein solution was stored at −80° C. until use.

FPT Activity Assay. FPT fractions were assayed using the Amersham Scintillation Proximity Assay (SPA) kit. Assays were performed at 23° C. in 200 μL with biotinylated human K-Ras-4B C-terminal peptide KKSKTKCVIM (100 nM) and [1-³H]-FPP (90 nM) as substrates in a buffer of 50 mM Tris, pH 7.7, 5 mM MgCl₂, 5 μM ZnCl₂, 0.01% Triton X-100, 0.2 mg/ml BSA and 2 mM DTT. Reactions were initiated by adding FPT fractions (25 to 250 ng) to the substrate mixture. The reaction mixture was incubated for 30 min before it was terminated by 3 reaction volumes of a quench solution containing 5 mg/mL scintillation beads, 500 mM EDTA, pH 8.0, and 0.5% BSA. After rocking the quenched solution at room temperature for 30 min, the radioactivity incorporated into the product was directly counted in a 96-well plate format with a Wallac 1204 Betaplate BS liquid scintillation counter.

EXAMPLE 2 Co-Crystallization of FPT:αHFP:Peptide Complexes

Purified rat FPT was dialyzed against 20 mM Tris pH 7.7, 1 mM DTT, 20 mM KCl, 10 μM ZnCl₂ and concentrated to 0.27 mM (25 mg/mL) and stored at −30° C. prior to crystallization. The Ac-Cys-Val-Ile-selenoMet-COOH:αHFP: FPT(CVIM:αHFP:FPT) ternary complex was prepared by incubating 108 μM FPT (10 mg/ml) with 300 μM αHFP (Calbiochem-Novabiochem Corporation) for about 2 hours prior to adding 300 μM Ac-Cys-Val-Ile-Met(Se)-COOH (AnaSpec Inc.). αHFP was added from a 23.6 mM solution in ethanol, yielding 0.6% (v/v) ethanol in the final solution. The peptide was added from a 50 mM solution in DMSO, resulting in a 0.3% (v/v) final DMSO concentration. The ternary mixture was incubated at 4° C. for approximately 4 hours. Vapor diffusion crystallization experiments were conducted using the hanging drop method. Potential crystallization conditions were screened by sparse matrix sampling (Jancarik et al., 1991, J. Appl. Cryst. 24:409-411) and systematic grid screens (Cox et al, 1998, J. Cryst. Growth 90:318-324) using standard solutions (Hampton Research Inc.). Crystals formed when the reservoir contained polyethylene glycol (PEG) and sodium acetate. Crystals most suitable for structure determination grew when the droplet contained 4 μl of the αHFP:CVIM:FPT complex, 4 μl of the reservoir solution (7% PEG 4000, 0.1 M sodium acetate, pH 5.7) and 1 μl of 200 mM DTT. Crystallization trays were incubated at 22° C. and after 2-3 weeks, hexagonal rods (0.1 mm×0.3 mm) appeared. Crystals can also be grown with other combinations of FPP analogs and Ca₁a₂X (SEQ ID No: 4) peptides such as the following:

FPP or FPP Analog Ca₁a₂X (SEQ ID No: 4) Peptide HFP Ac-CVIM-COOH (SEQ ID NO: 1) FPP Ac-CVFM-COOH (SEQ ID NO: 3)

EXAMPLE 3 Co-crystallization of FPT:FPP:Inhibitor Complexes

Cocrystals of FPT:FPP:Inhibitor complexes were grown as described above by substituting FPP at 150 μM. for αHFP and the inhibitor at 150 μM for the CVIM (SEQ ID No: 1) peptide. The following are examples of inhibitors that have been used to form FPT:FPP:Inhibitor co-crystals:

SCH66381

WO 97/23478 SCH66701

WO 97/23478 SCH69132

WO 97/23478

Many FPT inhibitors that are not listed will also be able to be used to form crystals.

EXAMPLE 4 Formation of FPT:FPP:Inhibitor Complexes by Soaking Preformed Co-Crystals

The cocrystals of FPT with αHFP and the CVIM peptide or with FPP and an inhibitor as described above in Examples 2 and 3 can be used to soak FPT inhibitors. Crystals are harvested into the reservoir solution at 4° C. For each new inhibitor, crystals are transferred into reservoir solution supplemented with 10 μM ZnCl₂, 2 mM DTT, 100 μM FPP and 100 μM inhibitor. The complex is allowed to form for about 24 hours at 4° C. In the presence of FPP and inhibitors, the FPP analog and peptide or original inhibitor are displaced, allowing structure determination of the new inhibitor:FPP:FPT complex.

EXAMPLE 5 Data Collection

X-ray diffraction data were collected on FPT complexes formed by co-crystallization. Prior to data collection, crystals were taken from the crystallization droplet and flash frozen in liquid propane using a cryoprotectant consisting of the reservoir solution supplemented with 25% (v/v) glycerol. Crystals belong to space group P6₁. The unit cell parameters vary less than 2% between crystals and are approximately a=b=174.13 Å, c=69.71 Å, α=β=90°, γ=120°.

Data were acquired by oscillation photography on a Rigaku R-AXIS IIC phosphor imaging area detector mounted on a Rigaku RU200 rotating anode generator (Molecular Structure Corp.), operating at 50 kV and 100 mA. Measured intensities were integrated, scaled and merged using the HKL software package (Z. Otwinowski and W. Minor). Statistics from four selected crystals are shown in Table 1, below:

TABLE 1 Data and Refinement Statistics Example 2 Example 3 Example 3 Example 3 Crystallization (αHFP + (FPP + (FPP + (FPP + Method CVIM) SCH66381) SCH66701) SCH69132) Max 2.4 2.2 2.9 2.5 Resolution (Å) Linear 6.1 5.5 9.6 5.9 R-factor (%) Percent Complete 90.4 90.5 97.9 59.9 Structure Example 7 Example 8 Example 9 Example 10 Determination Method Structure Table 2 Table 3 Table 4 Table 5 Coordinates Refinement 21.5 22.3 19.5 21.0 R-Factor (%)

TABLE 2 The following table lists the atomic structure coordinates for FPT in complex with αHFP and CVIM as derived by X-ray diffraction from crystals of that complex. The following abbreviations are used in the table: “RES” refers to the amino acid, FPP, FPP analog, peptide or inhibitor that the atom belongs to. “Atom” refers to the element whose coordinates have been determined. Elements are defined by the first letter in the column except for zinc which is defined by the letters “ZIN”, bromine which is defined by the letters “BR” and chlorine which is defined by the letters “CL”. ”#” is a number to identify the amino acid, FPP, FPP analog, peptide or inhibitor. “X, Y, Z” is the crystal- lographically determined atomic position determined for each atom. “B” is a thermal factor that measures movement of the atom around its atomic center. “C” refers to the part of the complex the atom belongs to. A = alpha subunit of FPT. B = beta subunit of FPT. Z = zinc atom. F = FPP, H = αHFP, I = FPT inhibitor; W = ordered solvent molecules, P = CVIM peptide. RES ATOM # X Y Z B C PHE CB 55 192.7 152.2 10.1 88 A PHE CG 55 192.8 153.3 9.1 90 A PHE CD1 55 193.7 153.3 8.1 91 A PHE CD2 55 191.8 154.4 9.2 91 A PHE CE1 55 193.8 154.4 7.2 92 A PHE CE2 55 191.9 155.4 8.3 92 A PHE CZ 55 192.9 155.4 7.2 92 A PHE C 55 194.1 153.1 12.0 83 A PHE O 55 194.8 154.1 11.7 83 A PHE N 55 194.0 150.7 11.6 85 A PHE CA 55 194.0 152.0 10.9 85 A LEU N 56 193.4 152.9 13.1 80 A LEU CA 56 193.5 153.9 14.2 77 A LEU CB 56 192.2 154.8 14.1 77 A LEU CG 56 192.4 156.3 14.5 76 A LEU CD1 56 191.2 157.1 14.1 75 A LEU CD2 56 192.7 156.5 16.0 75 A LEU C 56 193.5 153.1 15.5 75 A LEU O 56 192.5 152.4 15.9 74 A SER N 57 194.6 153.2 16.2 72 A SER CA 57 194.8 152.5 17.5 69 A SER CB 57 196.2 152.8 18.1 70 A SER OG 57 197.2 152.7 17.1 73 A SER C 57 193.8 152.7 18.6 67 A SER O 57 193.3 153.9 18.8 67 A LEU N 58 193.5 151.7 19.4 63 A LEU CA 58 192.6 151.8 20.5 60 A LEU CB 58 192.2 150.4 21.1 58 A LEU CG 58 191.0 149.7 20.6 56 A LEU CD1 58 191.0 148.4 21.3 56 A LEU CD2 58 189.8 150.4 20.9 55 A LEU C 58 193.3 152.6 21.6 60 A LEU O 58 192.7 153.2 22.4 59 A ASP N 59 194.7 152.6 21.5 60 A ASP CA 59 195.5 153.3 22.4 59 A ASP CB 59 196.7 152.4 22.7 62 A ASP CG 59 196.3 151.0 23.2 65 A ASP OD1 59 196.6 150.1 22.4 66 A ASP OD2 59 195.6 150.9 24.2 67 A ASP C 59 196.0 154.7 22.0 56 A ASP O 59 196.7 155.4 22.8 56 A SER N 60 195.7 155.1 20.7 52 A SER CA 60 196.1 156.4 20.2 49 A SER CB 60 195.7 156.5 18.8 49 A SER OG 60 195.9 157.8 18.3 48 A SER C 60 195.5 157.5 21.1 47 A SER O 60 194.3 157.4 21.4 47 A PRO N 61 196.3 158.5 21.3 45 A PRO CD 61 197.6 158.8 20.8 44 A PRO CA 61 195.8 159.7 22.1 43 A PRO CB 61 197.0 160.6 22.2 43 A PRO CG 61 197.7 160.3 20.9 44 A PRO C 61 194.6 160.4 21.4 42 A PRO O 61 193.8 161.1 22.0 40 A THR N 62 194.6 160.2 20.1 41 A THR CA 62 193.6 160.8 19.2 42 A THR CB 62 194.2 161.6 18.1 41 A THR OG1 62 195.0 160.8 17.2 41 A THR CG2 62 195.1 162.7 18.7 40 A THR C 62 192.6 159.7 18.7 42 A THR O 62 192.2 159.8 17.5 43 A TYR N 63 192.3 158.8 19.5 41 A TYR CA 63 191.3 157.7 19.1 39 A TYR CB 63 191.5 156.5 20.1 37 A TYR CG 63 190.4 155.5 19.9 35 A TYR CD1 63 190.5 154.5 18.9 35 A TYR CE1 63 189.5 153.5 18.7 35 A TYR CD2 63 189.2 155.5 20.7 35 A TYR CE2 63 188.2 154.5 20.5 35 A TYR CZ 63 188.4 153.6 19.5 34 A TYR OH 63 187.4 152.6 19.3 34 A TYR C 63 189.9 158.3 19.3 40 A TYR O 63 189.6 158.9 20.3 40 A VAL N 64 189.1 158.1 18.3 40 A VAL CA 64 187.7 158.5 18.4 40 A VAL CB 64 187.4 159.5 17.3 40 A VAL CG1 64 188.1 160.8 17.5 40 A VAL CG2 64 187.7 159.0 15.9 39 A VAL C 64 186.7 157.4 18.3 40 A VAL O 64 186.9 156.4 17.5 40 A LEU N 65 185.6 157.4 19.1 40 A LEU CA 65 184.6 156.4 19.1 39 A LEU CB 65 183.4 156.8 20.0 36 A LEU CG 65 183.9 157.1 21.5 36 A LEU CD1 65 182.7 157.5 22.3 36 A LEU CD2 65 184.6 156.0 22.1 34 A LEU C 65 184.0 156.3 17.7 42 A LEU O 65 183.9 157.2 16.9 43 A TYR N 66 183.6 155.0 17.4 44 A TYR CA 66 183.0 154.7 16.1 43 A TYR CB 66 182.6 153.2 16.0 41 A TYR CG 66 183.8 152.4 15.7 40 A TYR CD1 66 184.7 152.1 16.7 40 A TYR CE1 66 185.8 151.4 16.4 40 A TYR CD2 66 184.0 151.9 14.5 39 A TYR CE2 66 185.1 151.1 14.2 39 A TYR CZ 66 186.0 150.9 15.2 40 A TYR OH 66 187.1 150.1 14.9 40 A TYR C 66 181.7 155.6 15.9 43 A TYR O 66 181.5 156.0 14.7 44 A ARG N 67 181.0 155.9 16.9 44 A ARG CA 67 179.8 156.1 16.8 46 A ARG CB 67 179.0 156.8 18.1 46 A ARG CG 67 179.7 157.5 19.3 47 A ARG CD 67 178.7 157.7 20.4 48 A ARG NE 67 179.2 158.1 21.6 49 A ARG CZ 67 179.3 157.4 22.7 50 A ARG NH1 67 179.0 156.1 22.7 52 A ARG NH2 67 179.8 157.9 23.8 51 A ARG C 67 180.2 158.1 16.4 46 A ARG O 67 179.5 158.7 15.6 49 A ASP N 68 181.4 158.6 16.8 46 A ASP CA 68 181.9 159.9 16.3 45 A ASP CB 68 182.8 160.5 17.4 45 A ASP CG 68 182.1 160.9 18.6 46 A ASP OD1 68 180.8 161.1 18.6 47 A ASP OD2 68 182.7 161.1 19.7 47 A ASP C 68 182.6 159.8 15.0 45 A ASP O 68 183.2 160.8 14.6 47 A ARG N 69 182.5 158.7 14.3 45 A ARG CA 69 183.2 158.5 13.0 46 A ARG CB 69 183.9 157.2 12.9 46 A ARG CG 69 185.0 157.0 14.0 44 A ARG CD 69 185.9 155.8 13.8 41 A ARG NE 69 186.6 155.5 15.0 38 A ARG CZ 69 187.6 154.6 15.1 35 A ARG NH1 69 188.0 154.0 14.0 34 A ARG NH2 69 188.1 154.4 16.3 34 A ARG C 69 182.4 158.8 11.8 48 A ARG O 69 181.3 158.2 11.6 49 A ALA N 70 183.0 159.6 10.9 50 A ALA CA 70 182.4 160.0 9.6 52 A ALA CB 70 183.2 161.1 9.0 52 A ALA C 70 182.2 158.8 8.7 53 A ALA O 70 181.2 158.9 7.9 54 A GLU N 71 183.1 157.9 8.7 56 A GLU CA 71 183.0 156.7 7.7 58 A GLU CB 71 184.4 156.2 7.3 59 A GLU CG 71 185.3 155.7 8.5 62 A GLU CD 71 185.9 156.7 9.4 62 A GLU OE1 71 186.1 156.4 10.6 63 A GLU OE2 71 186.2 157.9 9.0 63 A GLU C 71 182.1 155.6 8.3 58 A GLU O 71 182.0 154.5 7.7 58 A TRP N 72 181.6 155.9 9.5 59 A TRP CA 72 180.7 154.9 10.3 61 A TRP CB 72 181.5 154.4 11.5 60 A TRP CG 72 182.5 153.3 11.2 58 A TRP CD2 72 182.2 151.9 11.1 57 A TRP CE2 72 183.4 151.3 10.8 58 A TRP CE3 72 181.0 151.2 11.1 57 A TRP CD1 72 183.8 153.5 11.0 58 A TRP NE1 72 184.4 152.2 10.7 58 A TRP CZ2 72 183.5 149.9 10.6 57 A TRP CZ3 72 181.1 149.8 10.9 56 A TRP CH2 72 182.3 149.2 10.7 56 A TRP C 72 179.4 155.6 10.7 62 A TRP O 72 179.1 155.6 11.9 62 A ALA N 73 178.7 156.3 9.8 64 A ALA CA 73 177.5 157.0 10.1 65 A ALA CB 73 177.7 158.5 9.8 66 A ALA C 73 176.3 156.4 9.4 64 A ALA O 73 175.1 156.6 9.8 64 A ASP N 74 176.6 155.7 8.3 64 A ASP CA 74 175.5 155.1 7.5 63 A ASP CB 74 176.1 154.7 6.1 63 A ASP CG 74 177.3 153.8 6.2 62 A ASP OD1 74 177.1 152.5 6.0 62 A ASP OD2 74 178.4 154.2 6.4 62 A ASP C 74 175.0 153.9 8.3 63 A ASP O 74 173.9 153.4 8.0 64 A ILE N 75 175.8 153.4 9.3 62 A ILE CA 75 175.4 152.2 10.1 61 A ILE CB 75 176.6 151.3 10.3 61 A ILE CG2 75 176.1 150.0 11.0 61 A ILE CG1 75 177.2 150.9 9.0 60 A ILE CD1 75 178.4 150.1 9.1 61 A ILE C 75 174.8 152.6 11.4 61 A ILE O 75 175.3 153.7 12.0 61 A ASP N 76 173.9 151.8 11.9 61 A ASP CA 76 173.3 152.1 13.3 60 A ASP CB 76 171.8 151.9 13.2 63 A ASP CG 76 171.1 153.1 12.4 65 A ASP OD1 76 170.6 152.9 11.3 65 A ASP OD2 76 171.0 154.2 13.0 65 A ASP C 76 173.9 151.0 14.2 59 A ASP O 76 173.9 149.8 13.9 59 A PRO N 77 174.5 151.4 15.3 57 A PRO CD 77 174.8 152.8 15.6 56 A PRO CA 77 175.1 150.5 16.3 55 A PRO CB 77 175.8 151.5 17.2 56 A PRO CG 77 175.0 152.7 17.1 56 A PRO C 77 174.1 149.7 17.0 55 A PRO O 77 173.2 150.2 17.7 55 A VAL N 78 174.2 148.4 16.8 53 A VAL CA 78 173.2 147.4 17.4 51 A VAL CB 78 173.2 146.1 16.6 52 A VAL CG1 78 172.2 145.1 17.2 51 A VAL CG2 78 172.8 146.4 15.2 51 A VAL C 78 173.8 147.1 18.8 52 A VAL O 78 174.9 146.5 18.9 52 A PRO N 79 173.1 147.5 19.8 52 A PRO CD 79 171.9 148.4 19.7 51 A PRO CA 79 173.4 147.3 21.2 52 A PRO CB 79 172.5 148.3 21.9 52 A PRO CG 79 171.3 148.2 21.1 52 A PRO C 79 173.2 145.9 21.7 53 A PRO O 79 172.3 145.2 21.1 54 A GLN N 80 173.8 145.5 22.8 54 A GLN CA 80 173.6 144.2 23.3 54 A GLN CB 80 174.7 143.8 24.3 53 A GLN CG 80 174.8 142.3 24.5 53 A GLN CD 80 176.0 141.9 25.3 54 A GLN OE1 80 176.3 142.3 26.4 55 A GLN NE2 80 176.8 141.1 24.6 55 A GLN C 80 172.3 144.1 24.0 55 A GLN O 80 171.8 145.0 24.6 57 A ASN N 81 171.6 142.9 23.8 56 A ASN CA 81 170.3 142.6 24.3 56 A ASN CB 81 169.4 142.1 23.2 58 A ASN CG 81 168.0 141.8 23.8 60 A ASN OD1 81 167.5 142.3 24.8 59 A ASN ND2 81 167.3 140.9 23.1 61 A ASN C 81 170.5 141.6 25.4 55 A ASN O 81 170.4 140.4 25.2 54 A ASP N 82 170.7 142.1 26.7 54 A ASP CA 82 170.8 141.2 27.9 54 A ASP CB 82 171.7 141.9 28.9 53 A ASP CG 82 173.2 141.8 28.4 53 A ASP OD1 82 173.5 141.4 27.3 52 A ASP OD2 82 174.0 142.3 29.3 53 A ASP C 82 169.5 140.9 28.5 55 A ASP O 82 169.4 140.3 29.6 54 A GLY N 83 168.4 141.4 28.0 56 A GLY CA 83 167.1 141.2 28.5 57 A GLY C 83 166.7 142.2 29.6 57 A GLY O 83 167.6 142.7 30.4 58 A PRO N 84 165.4 142.6 29.7 57 A PRO CD 84 164.4 141.9 28.9 56 A PRO CA 84 164.9 143.5 30.6 56 A PRO CB 84 163.4 143.3 30.4 57 A PRO CG 84 163.2 141.9 29.9 57 A PRO C 84 165.3 143.4 32.1 56 A PRO O 84 165.2 144.3 32.9 57 A SER N 85 165.8 142.2 32.4 56 A SER CA 85 166.3 142.0 33.8 56 A SER CB 85 165.2 141.2 34.5 57 A SER OG 85 163.9 141.6 34.2 60 A SER C 85 167.6 141.2 33.7 55 A SER O 85 167.6 140.0 33.6 55 A PRO N 86 168.7 141.9 33.6 54 A PRO CD 86 168.7 143.4 33.4 54 A PRO CA 86 170.1 141.4 33.5 52 A PRO CB 86 170.9 142.6 33.2 53 A PRO CG 86 169.9 143.6 32.5 53 A PRO C 86 170.6 140.6 34.6 49 A PRO O 86 170.2 140.8 35.8 49 A VAL N 87 171.6 139.7 34.3 46 A VAL CA 87 172.3 138.9 35.3 43 A VAL CB 87 171.7 137.4 35.4 44 A VAL CG1 87 170.5 137.4 36.3 44 A VAL CG2 87 171.3 136.9 34.0 43 A VAL C 87 173.7 138.9 34.8 42 A VAL O 87 173.9 139.1 33.6 42 A VAL N 88 174.7 138.6 35.7 41 A VAL CA 88 176.1 138.7 35.5 39 A VAL CB 88 176.7 137.3 35.1 38 A VAL CG1 88 176.8 136.5 36.4 37 A VAL CG2 88 176.0 136.6 34.0 37 A VAL C 88 176.3 139.6 34.3 41 A VAL O 88 176.8 139.3 33.2 42 A GLN N 89 175.8 140.9 34.5 41 A GLN CA 89 175.9 141.9 33.5 42 A GLN CB 89 174.7 142.8 33.7 42 A GLN CG 89 174.7 144.1 33.2 44 A GLN CD 89 173.6 144.9 33.8 46 A GLN OE1 89 173.4 144.9 35.0 46 A GLN NE2 89 172.8 145.6 33.0 46 A GLN C 89 177.2 142.8 33.7 42 A GLN O 89 177.4 143.4 34.8 43 A ILE N 90 178.0 142.8 32.7 42 A ILE CA 90 179.3 143.6 32.8 42 A ILE CB 90 180.3 143.0 31.8 40 A ILE CG2 90 181.7 143.5 32.1 40 A ILE CG1 90 180.3 141.4 31.9 39 A ILE CD1 90 180.9 140.7 30.8 37 A ILE C 90 179.1 145.1 32.4 44 A ILE O 90 178.3 145.4 31.5 45 A ILE N 91 179.7 146.0 33.2 46 A ILE CA 91 179.6 147.4 33.0 45 A ILE CB 91 179.6 148.2 34.3 46 A ILE CG2 91 179.6 149.7 34.0 46 A ILE CG1 91 178.5 147.9 35.3 46 A ILE CD1 91 177.1 148.1 34.6 47 A ILE C 91 180.7 147.7 32.1 44 A ILE O 91 181.8 148.0 32.6 42 A TYR N 92 180.5 147.7 30.8 44 A TYR CA 92 181.5 147.9 29.8 43 A TYR CB 92 181.1 147.5 28.4 42 A TYR CG 92 180.5 146.2 28.3 42 A TYR CD1 92 179.2 146.0 27.8 42 A TYR CE1 92 178.5 144.8 27.7 41 A TYR CD2 92 181.1 145.0 28.7 41 A TYR CE2 92 180.5 143.7 28.6 41 A TYR CZ 92 179.2 143.6 28.1 40 A TYR OH 92 178.6 142.4 28.0 39 A TYR C 92 181.8 149.4 29.8 43 A TYR O 92 181.0 150.2 30.3 44 A SER N 93 183.0 149.7 29.4 44 A SER CA 93 183.5 151.1 29.3 45 A SER CB 93 185.0 151.1 29.1 45 A SER OG 93 185.4 150.1 28.2 46 A SER C 93 182.8 151.6 28.0 45 A SER O 93 182.3 150.9 27.2 46 A GLU N 94 182.8 152.9 27.9 45 A GLU CA 94 182.1 153.5 26.7 47 A GLU CB 94 182.2 155.1 26.8 49 A GLU CG 94 181.1 155.8 26.0 52 A GLU CD 94 179.8 155.8 26.7 54 A GLU OE1 94 178.7 155.7 26.0 54 A GLU OE2 94 179.7 155.9 28.0 54 A GLU C 94 182.8 153.1 25.5 46 A GLU O 94 182.2 152.9 24.4 46 A LYS N 95 184.1 152.8 25.6 45 A LYS CA 95 184.9 152.4 24.5 43 A LYS CB 95 186.4 152.6 24.7 43 A LYS CG 95 187.2 152.8 23.5 43 A LYS CD 95 188.5 153.4 23.7 43 A LYS CE 95 189.5 152.3 24.2 43 A LYS NZ 95 190.8 152.9 24.0 43 A LYS C 95 184.7 150.9 24.1 42 A LYS O 95 184.6 150.6 22.9 42 A PHE N 96 184.5 150.0 25.1 41 A PHE CA 96 184.2 148.6 24.8 39 A PHE CB 96 184.3 147.8 26.1 36 A PHE CG 96 184.3 146.3 26.0 35 A PHE CD1 96 185.4 145.6 26.1 35 A PHE CD2 96 183.1 145.7 25.7 35 A PHE CE1 96 185.4 144.2 25.9 33 A PHE CE2 96 183.0 144.3 25.6 34 A PHE CZ 96 184.2 143.6 25.7 34 A PHE C 96 182.9 148.5 24.2 39 A PHE O 96 182.7 147.8 23.2 39 A ARG N 97 181.9 149.1 24.8 39 A ARG CA 97 180.5 149.1 24.3 40 A ARG CB 97 179.6 150.0 25.2 43 A ARG CG 97 178.6 149.2 26.0 48 A ARG CD 97 177.6 150.1 26.7 52 A ARG NE 97 178.3 151.0 27.6 56 A ARG CZ 97 178.7 152.3 27.3 57 A ARG NH1 97 178.4 152.8 26.1 58 A ARG NH2 97 179.3 153.0 28.2 58 A ARG C 97 180.4 149.7 22.9 39 A ARG O 97 179.7 149.2 22.1 39 A ASP N 98 181.2 150.8 22.7 38 A ASP CA 98 181.1 151.4 21.3 37 A ASP CB 98 181.9 152.7 21.4 37 A ASP CG 98 182.1 153.3 20.0 38 A ASP OD1 98 181.2 153.8 19.4 39 A ASP OD2 98 183.3 153.3 19.5 39 A ASP C 98 181.5 150.5 20.2 36 A ASP O 98 180.7 150.2 19.3 36 A VAL N 99 182.7 149.9 20.3 34 A VAL CA 99 183.3 149.0 19.3 32 A VAL CB 99 184.7 148.4 19.6 31 A VAL CG1 99 185.0 147.2 18.8 30 A VAL CG2 99 185.8 149.5 19.4 29 A VAL C 99 182.3 147.8 19.1 33 A VAL O 99 181.9 147.4 17.9 34 A TYR N 100 181.8 147.2 20.2 33 A TYR CA 100 180.9 146.1 20.1 35 A TYR CB 100 180.9 145.3 21.4 33 A TYR CG 100 182.0 144.3 21.5 32 A TYR CD1 100 183.2 144.7 22.1 31 A TYR CE1 100 184.3 143.8 22.1 30 A TYR CD2 100 181.9 143.0 20.9 31 A TYR CE2 100 183.0 142.2 21.0 31 A TYR CZ 100 184.2 142.5 21.5 30 A TYR OH 100 185.2 141.7 21.5 29 A TYR C 100 179.5 146.3 19.5 37 A TYR O 100 179.0 145.4 18.9 39 A ASP N 101 179.0 147.5 19.8 38 A ASP CA 101 177.7 147.9 19.3 37 A ASP CB 101 177.2 149.3 19.8 39 A ASP CG 101 176.5 149.2 21.2 40 A ASP OD1 101 176.5 148.2 21.9 41 A ASP OD2 101 176.0 150.3 21.6 42 A ASP C 101 177.8 147.9 17.8 37 A ASP O 101 176.9 147.5 17.0 35 A TYR N 102 179.0 148.3 17.3 36 A TYR CA 102 179.3 148.4 15.9 36 A TYR CB 102 180.4 149.3 15.6 39 A TYR CG 102 179.9 150.7 15.5 40 A TYR CD1 102 179.4 151.2 14.2 41 A TYR CE1 102 178.8 152.4 14.1 42 A TYR CD2 102 179.7 151.6 16.6 41 A TYR CE2 102 179.0 152.8 16.5 41 A TYR CZ 102 178.6 153.2 15.3 42 A TYR OH 102 177.9 154.4 15.1 43 A TYR C 102 179.6 147.0 15.4 36 A TYR O 102 179.3 146.7 14.2 37 A PHE N 103 180.1 146.1 16.2 36 A PHE CA 103 180.4 144.8 15.8 36 A PHE CB 103 181.3 144.0 16.7 34 A PHE CG 103 181.6 142.6 16.2 34 A PHE CD1 103 182.6 142.4 15.3 34 A PHE CD2 103 180.8 141.5 16.6 34 A PHE CE1 103 182.9 141.1 14.8 33 A PHE CE2 103 181.1 140.2 16.1 33 A PHE CZ 103 182.1 140.0 15.2 33 A PHE C 103 179.1 144.0 15.5 38 A PHE O 103 178.9 143.3 14.5 37 A ARG N 104 178.2 144.1 16.5 40 A ARG CA 104 176.9 143.5 16.4 42 A ARG CB 104 176.0 143.9 17.6 43 A ARG CG 104 176.5 143.4 18.9 45 A ARG CD 104 176.0 144.1 20.1 46 A ARG NE 104 176.7 143.6 21.3 49 A ARG CZ 104 177.1 144.4 22.3 51 A ARG NH1 104 177.0 145.7 22.3 51 A ARG NH2 104 177.8 143.7 23.3 52 A ARG C 104 176.1 143.8 15.1 42 A ARG O 104 175.4 143.0 14.5 45 A ALA N 105 176.4 145.1 14.6 42 A ALA CA 105 175.7 145.6 13.4 42 A ALA CB 105 175.7 147.1 13.4 42 A ALA C 105 176.3 145.1 12.1 42 A ALA O 105 175.6 144.7 11.2 43 A VAL N 106 177.7 145.2 12.0 42 A VAL CA 106 178.4 144.7 10.9 42 A VAL CB 106 179.9 145.1 11.0 42 A VAL CG1 106 180.9 143.9 10.7 41 A VAL CG2 106 180.3 146.2 10.1 41 A VAL C 106 178.2 143.2 10.7 42 A VAL O 106 178.0 142.7 9.6 40 A LEU N 107 178.2 142.5 11.8 43 A LEU CA 107 178.0 141.1 11.8 44 A LEU CB 107 178.3 140.5 13.2 42 A LEU CG 107 178.0 139.0 13.5 40 A LEU CD1 107 178.8 138.2 12.6 40 A LEU CD2 107 178.2 138.6 14.9 39 A LEU C 107 176.6 140.8 11.4 48 A LEU O 107 176.3 140.0 10.5 48 A GLN N 108 175.7 141.5 12.1 51 A GLN CA 108 174.2 141.3 11.9 54 A GLN CB 108 173.5 142.3 12.7 57 A GLN CG 108 172.0 141.9 13.0 60 A GLN CD 108 171.2 143.1 13.4 62 A GLN OE1 108 170.8 143.3 14.5 64 A GLN NE2 108 170.9 143.9 12.3 63 A GLN C 108 173.9 141.5 10.4 55 A GLN O 108 173.1 140.8 9.8 56 A ARG N 109 174.6 142.5 9.8 54 A ARG CA 109 174.4 142.8 8.4 55 A ARG CB 109 175.0 144.1 8.0 57 A ARG CG 109 174.4 145.4 8.6 61 A ARG CD 109 175.2 146.5 8.0 64 A ARG NE 109 174.5 147.8 8.2 66 A ARG CZ 109 173.3 148.2 7.7 67 A ARG NH1 109 172.6 147.3 7.0 68 A ARG NH2 109 172.9 149.4 7.9 69 A ARG C 109 175.2 141.8 7.6 53 A ARG O 109 175.0 141.6 6.4 55 A ASP N 110 176.2 141.2 8.2 52 A ASP CA 110 177.1 140.2 7.5 50 A ASP CB 110 176.4 139.0 6.9 50 A ASP CG 110 177.4 137.9 6.5 50 A ASP OD1 110 178.6 138.0 6.7 50 A ASP OD2 110 176.9 136.9 5.9 52 A ASP C 110 177.9 141.1 6.5 50 A ASP O 110 178.1 140.7 5.3 50 A GLU N 111 178.2 142.3 6.9 49 A GLU CA 111 178.9 143.2 6.1 49 A GLU CB 111 178.8 144.6 6.7 48 A GLU CG 111 179.3 145.7 5.7 49 A GLU CD 111 179.6 147.0 6.3 50 A GLU OE1 111 180.8 147.2 6.5 49 A GLU OE2 111 178.7 147.8 6.5 50 A GLU C 111 180.3 142.7 6.0 48 A GLU O 111 181.0 142.7 7.0 50 A ARG N 112 180.7 142.1 4.9 47 A ARG CA 112 182.0 141.6 4.7 46 A ARG CB 112 182.0 140.3 3.9 45 A ARG CG 112 181.1 139.3 4.6 45 A ARG CD 112 181.1 138.0 3.8 46 A ARG NE 112 180.3 137.0 4.5 46 A ARG CZ 112 180.0 135.8 4.0 46 A ARG NH1 112 180.5 135.4 2.8 46 A ARG NH2 112 179.2 134.9 4.7 47 A ARG C 112 182.9 142.6 4.0 47 A ARG O 112 183.3 142.4 2.9 46 A SER N 113 183.2 143.7 4.8 48 A SER CA 113 183.9 144.8 4.2 48 A SER CB 113 183.1 146.1 4.4 48 A SER OG 113 183.1 146.4 5.8 48 A SER C 113 185.2 145.0 4.9 47 A SER O 113 185.4 144.6 6.1 47 A GLU N 114 186.1 145.8 4.3 47 A GLU CA 114 187.4 146.2 4.8 47 A GLU CB 114 188.1 147.0 3.8 48 A GLU CG 114 189.5 147.3 4.2 49 A GLU CD 114 190.3 146.2 4.7 50 A GLU OE1 114 190.9 146.2 5.8 50 A GLU OE2 114 190.4 145.2 3.9 51 A GLU C 114 187.3 146.9 6.1 46 A GLU O 114 188.1 146.8 7.0 47 A ARG N 115 186.2 147.8 6.3 44 A ARG CA 115 186.1 148.5 7.5 44 A ARG CB 115 185.1 149.6 7.4 45 A ARG CG 115 183.7 149.2 6.9 47 A ARG CD 115 182.7 150.2 7.3 48 A ARG NE 115 181.4 150.0 6.6 50 A ARG CZ 115 180.4 150.8 6.6 51 A ARG NH1 115 179.3 150.4 6.0 52 A ARG NH2 115 180.4 151.9 7.3 51 A ARG C 115 185.7 147.5 8.6 43 A ARG O 115 186.0 147.7 9.8 44 A ALA N 116 184.9 146.5 8.2 42 A ALA CA 116 184.4 145.5 9.2 41 A ALA CB 116 183.5 144.6 8.5 41 A ALA C 116 185.7 144.8 9.7 40 A ALA O 116 185.8 144.5 10.9 40 A PHE N 117 186.6 144.5 8.8 38 A PHE CA 117 187.8 143.8 9.0 37 A PHE CB 117 188.6 143.7 7.7 35 A PHE CG 117 189.9 142.9 7.8 33 A PHE CD1 117 189.9 141.5 8.1 32 A PHE CD2 117 191.1 143.5 7.7 33 A PHE CE1 117 191.0 140.8 8.2 31 A PHE CE2 117 192.3 142.8 7.8 31 A PHE CZ 117 192.3 141.5 8.0 31 A PHE C 117 188.6 144.6 10.1 36 A PHE O 117 189.0 144.0 11.1 37 A LYS N 118 188.9 145.8 9.8 35 A LYS CA 118 189.7 146.7 10.7 35 A LYS CB 118 189.8 148.1 10.1 37 A LYS CG 118 190.7 148.1 8.8 40 A LYS CD 118 191.0 149.5 8.2 43 A LYS CE 118 191.9 149.3 7.0 45 A LYS NZ 118 192.2 150.6 6.3 47 A LYS C 118 189.0 146.8 12.0 33 A LYS O 118 189.7 147.0 13.0 33 A LEU N 119 187.7 146.6 12.1 32 A LEU CA 119 187.0 146.7 13.4 31 A LEU CB 119 185.5 147.0 13.2 30 A LEU CG 119 184.5 146.9 14.3 29 A LEU CD1 119 184.7 147.8 15.5 28 A LEU CD2 119 183.1 147.2 13.7 30 A LEU C 119 187.1 145.4 14.3 30 A LEU O 119 187.0 145.5 15.5 31 A THR N 120 187.1 144.2 13.6 29 A THR CA 120 187.2 143.0 14.4 28 A THR CB 120 187.3 141.8 13.5 26 A THR OG1 120 188.3 141.9 12.5 26 A THR CG2 120 185.9 141.5 12.8 24 A THR C 120 188.5 143.1 15.2 30 A THR O 120 188.6 142.6 16.3 30 A ARG N 121 189.5 143.8 14.6 31 A ARG CA 121 190.8 144.0 15.2 32 A ARG CB 121 191.6 144.8 14.2 36 A ARG CG 121 193.1 144.5 14.2 41 A ARG CD 121 193.7 145.4 15.2 46 A ARG NE 121 194.8 146.1 14.5 52 A ARG CZ 121 195.3 147.3 14.9 56 A ARG NH1 121 196.3 147.9 14.3 59 A ARG NH2 121 194.8 147.9 16.0 57 A ARG C 121 190.7 144.7 16.5 32 A ARG O 121 191.4 144.3 17.4 33 A ASP N 122 189.8 145.7 16.5 31 A ASP CA 122 189.7 146.4 17.8 29 A ASP CB 122 189.0 147.8 17.5 29 A ASP CG 122 189.9 148.8 16.9 27 A ASP OD1 122 191.1 148.8 17.2 27 A ASP OD2 122 189.4 149.7 16.3 28 A ASP C 122 188.8 145.6 18.7 30 A ASP O 122 189.1 145.6 19.9 30 A ALA N 123 187.8 144.9 18.2 29 A ALA CA 123 187.0 144.0 19.0 28 A ALA CB 123 185.9 143.4 18.1 28 A ALA C 123 187.8 142.9 19.6 29 A ALA O 123 187.5 142.5 20.8 31 A ILE N 124 188.8 142.4 18.9 29 A ILE CA 124 189.6 141.3 19.4 28 A ILE CB 124 190.5 140.8 18.2 26 A ILE CG2 124 191.8 140.1 18.8 24 A ILE CG1 124 189.7 139.8 17.4 23 A ILE CD1 124 190.4 139.5 16.1 23 A ILE C 124 190.6 141.9 20.5 30 A ILE O 124 190.9 141.2 21.4 31 A GLU N 125 191.0 143.1 20.3 32 A GLU CA 125 191.9 143.7 21.3 34 A GLU CB 125 192.6 144.9 20.8 38 A GLU CG 125 193.6 145.4 21.8 44 A GLU CD 125 194.1 146.8 21.5 48 A GLU OE1 125 194.1 147.7 22.5 50 A GLU OE2 125 194.4 147.1 20.3 50 A GLU C 125 191.1 144.0 22.6 33 A GLU O 125 191.8 144.0 23.7 34 A LEU N 126 189.9 144.3 22.5 30 A LEU CA 126 189.0 144.6 23.7 26 A LEU CB 126 187.8 145.3 23.3 26 A LEU CG 126 188.1 146.8 22.9 25 A LEU CD1 126 186.8 147.4 22.3 24 A LEU CD2 126 188.6 147.6 24.1 24 A LEU C 126 188.7 143.3 24.4 26 A LEU O 126 188.6 143.3 25.6 28 A ASN N 127 188.6 142.2 23.7 25 A ASN CA 127 188.3 140.8 24.3 24 A ASN CB 127 186.9 140.6 24.6 23 A ASN CG 127 186.7 139.2 25.3 24 A ASN OD1 127 187.7 138.6 25.7 24 A ASN ND2 127 185.4 138.8 25.4 22 A ASN C 127 188.8 139.8 23.3 24 A ASN O 127 188.1 139.2 22.5 23 A ALA N 128 190.1 139.4 23.4 24 A ALA CA 128 190.7 138.5 22.5 22 A ALA CB 128 192.2 138.4 22.8 22 A ALA C 128 190.1 137.1 22.6 23 A ALA O 128 190.2 136.3 21.7 23 A ALA N 129 189.4 136.8 23.7 23 A ALA CA 129 188.8 135.6 24.0 22 A ALA CB 129 188.6 135.3 25.5 21 A ALA C 129 187.4 135.5 23.3 23 A ALA O 129 186.6 134.5 23.5 23 A ASN N 130 187.0 136.5 22.5 23 A ASN CA 130 185.7 136.5 21.9 23 A ASN CB 130 185.2 137.9 21.5 23 A ASN CG 130 183.8 137.9 21.1 25 A ASN OD1 130 183.5 137.3 20.0 27 A ASN ND2 130 182.9 138.5 21.8 24 A ASN C 130 185.9 135.7 20.6 24 A ASN O 130 186.3 136.2 19.5 24 A TYR N 131 185.5 134.4 20.7 23 A TYR CA 131 185.6 133.4 19.6 22 A TYR CB 131 185.4 132.0 20.1 20 A TYR CG 131 184.0 131.8 20.7 19 A TYR CD1 131 183.0 131.3 20.0 18 A TYR CE1 131 181.7 131.2 20.5 17 A TYR CD2 131 183.8 132.1 22.0 19 A TYR CE2 131 182.5 132.0 22.6 17 A TYR CZ 131 181.5 131.5 21.8 17 A TYR OH 131 180.3 131.4 22.4 17 A TYR C 131 184.7 133.7 18.3 24 A TYR O 131 185.0 133.3 17.2 26 A THR N 132 183.6 134.4 18.6 23 A THR CA 132 182.6 134.8 17.5 21 A THR CB 132 181.3 135.4 18.1 22 A THR OG1 132 180.7 134.5 19.0 22 A THR CG2 132 180.4 135.8 17.0 22 A THR C 132 183.3 135.8 16.6 21 A THR O 132 183.2 135.6 15.3 21 A VAL N 133 183.9 136.8 17.2 20 A VAL CA 133 184.6 137.8 16.4 19 A VAL CB 133 185.2 138.9 17.3 20 A VAL CG1 133 186.0 139.9 16.4 18 A VAL CG2 133 184.1 139.7 18.0 20 A VAL C 133 185.8 137.1 15.6 20 A VAL O 133 186.0 137.5 14.5 24 A TRP N 134 186.5 136.2 16.3 20 A TRP CA 134 187.6 135.5 15.6 20 A TRP CB 134 188.3 134.6 16.6 18 A TRP CG 134 189.3 135.2 17.4 17 A TRP CD2 134 190.6 135.7 16.9 17 A TRP CE2 134 191.3 136.3 17.9 17 A TRP CE3 134 191.2 135.8 15.6 18 A TRP CD1 134 189.3 135.5 18.7 17 A TRP NE1 134 190.5 136.1 19.0 16 A TRP CZ2 134 192.5 136.9 17.8 17 A TRP CZ3 134 192.4 136.4 15.4 17 A TRP CH2 134 193.1 136.9 16.5 18 A TRP C 134 187.1 134.7 14.4 24 A TRP O 134 187.8 134.6 13.4 26 A HIS N 135 185.8 134.2 14.5 28 A HIS CA 135 185.2 133.5 13.4 30 A HIS CB 135 184.0 132.8 13.9 33 A HIS CG 135 183.4 131.8 12.9 35 A HIS CD2 135 183.7 130.5 12.8 35 A HIS ND1 135 182.5 132.1 11.9 35 A HIS CE1 135 182.2 131.0 11.2 35 A HIS NE2 135 182.9 130.0 11.7 36 A HIS C 135 184.9 134.4 12.2 31 A HIS O 135 185.4 134.2 11.1 32 A PHE N 136 184.2 135.5 12.5 30 A PHE CA 136 183.8 136.5 11.5 29 A PHE CB 136 183.0 137.6 12.1 31 A PHE CG 136 182.5 138.6 11.0 33 A PHE CD1 136 181.5 138.2 10.1 33 A PHE CD2 136 182.9 139.9 11.0 34 A PHE CE1 136 181.0 139.2 9.2 32 A PHE CE2 136 182.4 140.9 10.1 34 A PHE CZ 136 181.4 140.5 9.2 32 A PHE C 136 185.1 137.0 10.8 29 A PHE O 136 185.1 137.3 9.6 32 A ARG N 137 186.2 137.1 11.6 28 A ARG CA 137 187.4 137.6 11.0 25 A ARG CB 137 188.5 137.9 12.0 24 A ARG CG 137 189.8 138.4 11.5 22 A ARG CD 137 190.8 138.8 12.5 23 A ARG NE 137 192.0 139.3 12.0 22 A ARG CZ 137 192.3 140.6 11.9 22 A ARG NH1 137 191.5 141.5 12.3 23 A ARG NH2 137 193.5 141.0 11.3 21 A ARG C 137 188.0 136.6 10.0 26 A ARG O 137 188.6 137.0 9.0 28 A ARG N 138 187.9 135.3 10.2 26 A ARG CA 138 188.4 134.3 9.3 26 A ARG CB 138 188.5 132.9 9.9 25 A ARG CG 138 189.7 132.8 10.8 24 A ARG CD 138 190.0 131.4 11.2 22 A ARG NE 138 189.1 130.9 12.2 21 A ARG CZ 138 189.2 131.1 13.5 21 A ARG NH1 138 190.2 131.8 14.0 23 A ARG NH2 138 188.4 130.5 14.3 21 A ARG C 138 187.6 134.4 8.0 27 A ARG O 138 188.1 134.2 6.9 28 A VAL N 139 186.3 134.6 8.2 29 A VAL CA 139 185.4 134.7 7.0 29 A VAL CB 139 183.9 135.0 7.5 29 A VAL CG1 139 183.0 135.2 6.3 28 A VAL CG2 139 183.4 133.9 8.4 27 A VAL C 139 185.9 135.9 6.2 30 A VAL O 139 186.0 135.8 4.9 29 A LEU N 140 186.1 137.0 6.8 29 A LEU CA 140 186.6 138.2 6.1 29 A LEU CB 140 186.7 139.4 7.0 28 A LEU CG 140 185.4 139.8 7.6 28 A LEU CD1 140 185.4 141.2 8.3 27 A LEU CD2 140 184.4 139.9 6.5 28 A LEU C 140 188.0 137.9 5.5 29 A LEU O 140 188.2 138.4 4.4 31 A LEU N 141 188.8 137.1 6.1 31 A LEU CA 141 190.1 136.7 5.5 32 A LEU CB 141 190.9 135.8 6.5 31 A LEU CG 141 191.6 136.5 7.6 29 A LEU CD1 141 192.3 135.4 8.4 29 A LEU CD2 141 192.6 137.5 7.1 28 A LEU C 141 189.9 136.1 4.2 34 A LEU O 141 190.6 136.3 3.2 33 A ARG N 142 188.9 135.2 4.1 37 A ARG CA 142 188.6 134.4 2.9 40 A ARG CB 142 187.8 133.2 3.2 44 A ARG CG 142 188.5 132.2 4.1 49 A ARG CD 142 187.6 131.1 4.7 53 A ARG NE 142 186.9 131.6 5.9 55 A ARG CZ 142 186.5 130.7 6.9 56 A ARG NH1 142 186.7 129.4 6.8 56 A ARG NH2 142 185.8 131.2 7.9 56 A ARG C 142 187.9 135.3 1.8 39 A ARG O 142 188.4 135.5 0.7 39 A SER N 143 186.8 135.9 2.3 38 A SER CA 143 186.0 136.8 1.4 36 A SER CB 143 184.9 137.3 2.2 34 A SER OG 143 184.2 138.3 1.4 36 A SER C 143 186.8 137.9 0.8 36 A SER O 143 187.1 138.0 −0.4 37 A LEU N 144 187.3 138.8 1.7 36 A LEU CA 144 188.1 140.0 1.2 35 A LEU CB 144 188.4 140.9 2.3 34 A LEU CG 144 187.3 141.4 3.3 35 A LEU CD1 144 187.9 142.4 4.3 36 A LEU CD2 144 186.2 141.9 2.6 36 A LEU C 144 189.4 139.5 0.6 36 A LEU O 144 190.2 140.3 0.1 38 A GLN N 145 189.7 138.2 0.6 36 A GLN CA 145 190.9 137.7 0.1 38 A GLN CB 145 190.9 137.8 −1.5 40 A GLN CG 145 190.0 136.8 −2.2 44 A GLN CD 145 190.8 135.9 −3.1 46 A GLN OE1 145 191.2 136.2 −4.2 48 A GLN NE2 145 191.1 134.6 −2.6 47 A GLN C 145 192.1 138.5 0.6 37 A GLN O 145 192.7 139.3 −0.1 38 A LYS N 146 192.3 138.3 1.9 36 A LYS CA 146 193.4 139.0 2.6 34 A LYS CB 146 193.1 139.3 4.0 34 A LYS CG 146 191.8 140.0 4.3 34 A LYS CD 146 191.8 141.4 3.7 35 A LYS CE 146 192.9 142.3 4.3 34 A LYS NZ 146 193.0 143.6 3.7 34 A LYS C 146 194.8 138.3 2.5 34 A LYS O 146 194.8 137.1 2.3 33 A ASP N 147 195.8 139.1 2.6 35 A ASP CA 147 197.2 138.5 2.5 35 A ASP CB 147 198.3 139.6 2.4 37 A ASP CG 147 199.7 139.0 2.3 39 A ASP OD1 147 200.0 138.1 3.0 41 A ASP OD2 147 200.5 139.5 1.5 41 A ASP C 147 197.3 137.8 3.9 36 A ASP O 147 197.4 138.4 4.9 36 A LEU N 148 197.4 136.5 3.8 34 A LEU CA 148 197.5 135.7 5.0 32 A LEU CB 148 197.1 134.2 4.7 29 A LEU CG 148 195.7 134.1 4.2 28 A LEU CD1 148 195.5 132.7 3.8 28 A LEU CD2 148 194.7 134.5 5.3 28 A LEU C 148 198.8 135.8 5.7 32 A LEU O 148 198.8 135.7 6.9 35 A GLN N 149 199.9 136.0 5.0 34 A GLN CA 149 201.2 136.1 5.6 35 A GLN CB 149 202.3 136.1 4.6 35 A GLN CG 149 203.6 135.6 5.1 39 A GLN CD 149 203.5 134.2 5.8 41 A GLN OE1 149 203.2 133.2 5.2 41 A GLN NE2 149 203.7 134.3 7.1 42 A GLN C 149 201.3 137.3 6.5 35 A GLN O 149 201.9 137.4 7.5 36 A GLU N 150 200.5 138.3 6.0 35 A GLU CA 150 200.4 139.6 6.7 35 A GLU CB 150 199.7 140.5 5.8 38 A GLU CG 150 199.8 142.0 6.2 45 A GLU CD 150 198.6 142.8 5.6 49 A GLU OE1 150 197.9 142.3 4.7 51 A GLU OE2 150 198.4 143.9 6.1 52 A GLU C 150 199.6 139.3 8.0 33 A GLU O 150 199.9 139.9 9.0 31 A GLU N 151 198.7 138.4 7.9 31 A GLU CA 151 197.8 138.0 9.0 31 A GLU CB 151 196.5 137.3 8.5 29 A GLU CG 151 195.7 136.8 9.7 27 A GLU CD 151 194.8 137.8 10.4 27 A GLU OE1 151 194.9 139.0 10.0 27 A GLU OE2 151 194.0 137.4 11.2 27 A GLU C 151 198.6 137.1 10.0 31 A GLU O 151 198.4 137.1 11.2 30 A MET N 152 199.6 136.4 9.4 29 A MET CA 152 200.4 135.5 10.3 29 A MET CB 152 201.4 134.7 9.4 28 A MET CG 152 201.0 133.4 9.0 30 A MET SD 152 200.9 132.1 10.3 29 A MET CE 152 202.6 132.3 10.9 30 A MET C 152 201.2 136.4 11.2 30 A MET O 152 201.3 136.1 12.4 31 A ASN N 153 201.6 137.6 10.7 30 A ASN CA 153 202.3 138.5 11.6 31 A ASN CB 153 202.8 139.7 10.7 33 A ASN CG 153 203.8 139.2 9.6 36 A ASN OD1 153 204.5 138.3 9.8 36 A ASN ND2 153 203.7 139.9 8.5 38 A ASN C 153 201.5 139.1 12.7 29 A ASN O 153 201.9 139.3 13.8 30 A TYR N 154 200.2 139.4 12.3 28 A TYR CA 154 199.2 139.9 13.3 25 A TYR CB 154 197.9 140.1 12.5 25 A TYR CG 154 196.7 140.3 13.5 26 A TYR CD1 154 196.5 141.5 14.1 26 A TYR CE1 154 195.5 141.7 15.0 26 A TYR CD2 154 195.8 139.3 13.7 27 A TYR CE2 154 194.8 139.4 14.6 27 A TYR CZ 154 194.6 140.7 15.2 27 A TYR OH 154 193.6 140.8 16.1 30 A TYR C 154 199.1 138.9 14.4 25 A TYR O 154 199.4 139.2 15.5 25 A ILE N 155 198.6 137.7 14.1 24 A ILE CA 155 198.4 136.6 15.1 23 A ILE CB 155 197.9 135.3 14.4 22 A ILE CG2 155 199.0 134.5 13.8 20 A ILE CG1 155 197.1 134.5 15.5 20 A ILE CD1 155 196.0 135.3 16.1 21 A ILE C 155 199.7 136.3 15.9 24 A ILE O 155 199.7 136.0 17.0 25 A THR N 156 200.9 136.6 15.2 22 A THR CA 156 202.2 136.3 15.9 20 A THR CB 156 203.3 136.6 15.0 19 A THR OG1 156 203.3 135.6 13.9 19 A THR CG2 156 204.6 136.6 15.7 18 A THR C 156 202.3 137.3 17.1 22 A THR O 156 202.7 136.9 18.1 23 A ALA N 157 202.0 138.6 16.8 23 A ALA CA 157 202.0 139.6 17.8 23 A ALA CB 157 201.9 141.0 17.2 22 A ALA C 157 201.0 139.4 18.9 24 A ALA O 157 201.3 139.6 20.1 26 A ILE N 158 199.8 139.1 18.5 24 A ILE CA 158 198.7 138.8 19.5 22 A ILE CB 158 197.3 138.5 18.7 22 A ILE CG2 158 196.2 138.3 19.7 22 A ILE CG1 158 196.9 139.7 17.9 22 A ILE CD1 158 196.4 140.9 18.7 23 A ILE C 158 199.0 137.7 20.4 22 A ILE O 158 198.6 137.8 21.6 24 A ILE N 159 199.6 136.6 19.9 21 A ILE CA 159 199.9 135.5 20.7 20 A ILE CB 159 200.4 134.3 19.9 20 A ILE CG2 159 200.9 133.1 20.8 20 A ILE CG1 159 199.3 133.7 19.0 18 A ILE CD1 159 199.8 132.7 18.0 16 A ILE C 159 201.0 135.8 21.7 22 A ILE O 159 201.0 135.4 22.8 22 A GLU N 160 201.9 136.7 21.3 24 A GLU CA 160 203.0 137.1 22.2 24 A GLU CB 160 204.0 138.1 21.5 24 A GLU CG 160 204.9 137.5 20.4 26 A GLU CD 160 206.1 136.7 20.8 27 A GLU OE1 160 206.4 136.6 22.0 29 A GLU OE2 160 206.7 136.0 20.0 27 A GLU C 160 202.4 137.8 23.3 23 A GLU O 160 202.8 137.7 24.5 23 A GLU N 161 201.2 138.4 23.1 24 A GLU CA 161 200.5 139.2 24.1 25 A GLU CB 161 199.7 140.3 23.4 25 A GLU CG 161 200.6 141.4 22.9 27 A GLU CD 161 199.8 142.3 22.0 29 A GLU OE1 161 200.5 143.2 21.4 30 A GLU OE2 161 198.6 142.2 21.9 29 A GLU C 161 199.6 138.3 25.0 25 A GLU O 161 199.6 138.6 26.2 27 A GLN N 162 199.0 137.3 24.5 26 A GLN CA 162 198.1 136.4 25.2 25 A GLN CB 162 196.6 136.7 24.7 27 A GLN CG 162 196.5 138.1 24.3 30 A GLN CD 162 195.5 138.8 25.1 34 A GLN OE1 162 195.1 138.3 26.2 35 A GLN NE2 162 195.1 140.0 24.7 36 A GLN C 162 198.4 135.0 24.8 24 A GLN O 162 197.6 134.3 24.1 24 A PRO N 163 199.5 134.5 25.2 23 A PRO CD 163 200.5 135.1 26.1 22 A PRO CA 163 200.0 133.1 24.8 22 A PRO CB 163 201.4 133.1 25.3 22 A PRO CG 163 201.4 133.9 26.5 21 A PRO C 163 199.2 132.0 25.5 23 A PRO O 163 199.5 130.8 25.3 24 A LYS N 164 198.2 132.3 26.3 23 A LYS CA 164 197.3 131.4 27.0 23 A LYS CB 164 197.5 131.5 28.5 26 A LYS CG 164 198.8 131.0 29.0 30 A LYS CD 164 198.6 130.9 30.5 33 A LYS CE 164 199.8 130.2 31.1 36 A LYS NZ 164 199.5 130.0 32.5 39 A LYS C 164 195.9 131.4 26.5 22 A LYS O 164 195.0 130.9 27.2 22 A ASN N 165 195.7 132.1 25.4 21 A ASN CA 165 194.4 132.3 24.9 18 A ASN CB 165 194.3 133.7 24.2 17 A ASN CG 165 193.1 133.9 23.3 18 A ASN OD1 165 192.9 133.2 22.3 19 A ASN ND2 165 192.3 134.8 23.7 18 A ASN C 165 194.2 131.1 23.9 17 A ASN O 165 195.1 130.8 23.2 17 A TYR N 166 193.0 130.5 23.9 16 A TYR CA 166 192.7 129.4 23.1 15 A TYR CB 166 191.5 128.7 23.6 14 A TYR CG 166 191.7 127.7 24.7 15 A TYR CD1 166 191.7 128.1 26.0 14 A TYR CE1 166 191.9 127.2 27.0 14 A TYR CD2 166 191.7 126.3 24.4 15 A TYR CE2 166 191.9 125.4 25.4 15 A TYR CZ 166 191.9 125.8 26.7 15 A TYR OH 166 192.1 124.9 27.8 15 A TYR C 166 192.5 129.8 21.6 16 A TYR O 166 192.8 129.0 20.7 16 A GLN N 167 191.8 130.9 21.4 17 A GLN CA 167 191.5 131.3 20.0 17 A GLN CB 167 190.5 132.5 20.1 18 A GLN CG 167 189.1 132.1 20.6 21 A GLN CD 167 189.1 131.8 22.0 23 A GLN OE1 167 189.7 132.5 22.8 26 A GLN NE2 167 188.5 130.7 22.4 24 A GLN C 167 192.6 131.7 19.1 17 A GLN O 167 192.6 131.5 17.9 17 A VAL N 168 193.6 132.4 19.7 18 A VAL CA 168 194.8 132.9 19.0 17 A VAL CB 168 195.6 133.8 19.9 17 A VAL CG1 168 194.9 135.1 20.2 15 A VAL CG2 168 196.0 133.2 21.2 15 A VAL C 168 195.6 131.7 18.5 21 A VAL O 168 196.1 131.8 17.3 24 A TRP N 169 195.8 130.7 19.2 21 A TRP CA 169 196.6 129.5 18.8 20 A TRP CB 169 196.9 128.6 19.9 20 A TRP CG 169 197.9 129.1 20.8 19 A TRP CD2 169 199.3 129.0 20.5 18 A TRP CE2 169 200.0 129.6 21.7 18 A TRP CE3 169 200.1 128.6 19.5 16 A TRP CD1 169 197.8 129.6 22.0 18 A TRP NE1 169 199.0 130.0 22.5 19 A TRP CZ2 169 201.4 129.7 21.7 17 A TRP CZ3 169 201.5 128.7 19.6 16 A TRP CH2 169 202.1 129.2 20.7 16 A TRP C 169 195.8 128.8 17.7 22 A TRP O 169 196.4 128.4 16.7 23 A HIS N 170 194.5 128.6 17.9 23 A HIS CA 170 193.7 128.0 16.9 24 A HIS CB 170 192.3 127.8 17.3 24 A HIS CG 170 191.5 127.1 16.3 24 A HIS CD2 170 190.4 127.5 15.6 25 A HIS ND1 170 191.8 125.8 15.8 25 A HIS CE1 170 190.9 125.5 14.9 25 A HIS NE2 170 190.1 126.5 14.7 25 A HIS C 170 193.7 128.8 15.6 26 A HIS O 170 193.6 128.2 14.5 28 A HIS N 171 193.6 130.1 15.7 24 A HIS CA 171 193.6 130.9 14.5 22 A HIS CB 171 193.4 132.4 14.9 22 A HIS CG 171 193.3 133.3 13.8 22 A HIS CD2 171 194.3 134.1 13.2 22 A HIS ND1 171 192.1 133.6 13.2 21 A HIS CE1 171 192.3 134.6 12.2 20 A HIS NE2 171 193.6 134.9 12.2 21 A HIS C 171 194.9 130.8 13.7 23 A HIS O 171 194.9 130.7 12.5 24 A ARG N 172 196.0 130.7 14.4 23 A ARG CA 172 197.3 130.5 13.8 22 A ARG CB 172 198.4 130.6 14.9 21 A ARG CG 172 199.8 130.3 14.3 20 A ARG CD 172 200.9 130.7 15.2 19 A ARG NE 172 202.2 130.6 14.6 19 A ARG CZ 172 202.9 131.7 14.3 20 A ARG NH1 172 202.6 132.9 14.6 20 A ARG NH2 172 204.1 131.5 13.7 20 A ARG C 172 197.4 129.2 13.1 25 A ARG O 172 198.0 129.1 12.0 25 A ARG N 173 196.8 128.1 13.7 26 A ARG CA 173 196.8 126.8 13.2 26 A ARG CB 173 196.3 125.8 14.2 27 A ARG CG 173 195.6 124.6 13.6 28 A ARG CD 173 195.8 123.4 14.4 30 A ARG NE 173 195.1 122.3 13.8 35 A ARG CZ 173 194.9 121.1 14.2 36 A ARG NH1 173 195.4 120.7 15.4 37 A ARG NH2 173 194.2 120.2 13.5 36 A ARG C 173 196.1 126.8 11.9 26 A ARG O 173 196.4 126.1 10.9 28 A VAL N 174 195.0 127.5 11.8 25 A VAL CA 174 194.1 127.6 10.6 24 A VAL CB 174 192.8 128.4 10.9 22 A VAL CG1 174 192.1 128.7 9.6 22 A VAL CG2 174 191.9 127.5 11.7 20 A VAL C 174 194.9 128.3 9.5 25 A VAL O 174 194.9 127.8 8.4 28 A LEU N 175 195.5 129.4 9.8 26 A LEU CA 175 196.3 130.1 8.7 27 A LEU CB 175 197.0 131.3 9.3 27 A LEU CG 175 196.1 132.5 9.9 25 A LEU CD1 175 197.0 133.6 10.4 24 A LEU CD2 175 195.2 133.0 8.8 24 A LEU C 175 197.4 129.2 8.2 27 A LEU O 175 197.6 129.2 6.9 30 A VAL N 176 198.2 128.5 9.0 27 A VAL CA 176 199.2 127.6 8.6 26 A VAL CB 176 200.0 127.0 9.8 24 A VAL CG1 176 201.0 126.0 9.4 24 A VAL CG2 176 200.6 128.1 10.6 23 A VAL C 176 198.7 126.5 7.7 27 A VAL O 176 199.3 126.0 6.8 28 A GLU N 177 197.4 126.1 8.0 28 A GLU CA 177 196.8 125.0 7.2 30 A GLU CB 177 195.6 124.5 7.9 30 A GLU CG 177 195.9 123.6 9.2 31 A GLU CD 177 194.6 123.2 9.9 32 A GLU OE1 177 194.6 122.2 10.5 34 A GLU OE2 177 193.6 124.0 9.8 33 A GLU C 177 196.5 125.6 5.8 31 A GLU O 177 196.8 125.1 4.8 33 A TRP N 178 195.9 126.8 5.8 30 A TRP CA 178 195.5 127.5 4.6 29 A TRP CB 178 194.9 128.9 4.9 27 A TRP CG 178 193.5 128.9 5.4 25 A TRP CD2 178 192.8 130.1 6.0 24 A TRP CE2 178 191.5 129.7 6.3 24 A TRP CE3 178 193.2 131.4 6.2 24 A TRP CD1 178 192.5 127.9 5.4 24 A TRP NE1 178 191.3 128.3 5.9 24 A TRP CZ2 178 190.5 130.6 6.8 24 A TRP CZ3 178 192.2 132.3 6.8 24 A TRP CH2 178 190.9 131.8 7.1 24 A TRP C 178 196.7 127.6 3.7 31 A TRP O 178 196.6 127.3 2.5 33 A LEU N 179 197.8 128.1 4.3 32 A LEU CA 179 199.0 128.3 3.6 33 A LEU CB 179 199.9 129.3 4.3 31 A LEU CG 179 199.3 130.7 4.5 32 A LEU CD1 179 200.1 131.4 5.6 32 A LEU CD2 179 199.5 131.5 3.2 32 A LEU C 179 199.8 127.0 3.4 35 A LEU O 179 200.7 127.0 2.4 36 A LYS N 180 199.6 126.0 4.2 37 A LYS CA 180 200.4 124.8 4.1 39 A LYS CB 180 200.2 124.1 2.7 40 A LYS CG 180 198.9 123.4 2.4 43 A LYS CD 180 198.0 124.4 1.6 46 A LYS CE 180 196.6 123.8 1.4 48 A LYS NZ 180 195.6 124.8 0.9 50 A LYS C 180 201.9 125.1 4.2 38 A LYS O 180 202.8 124.6 3.6 40 A ASP N 181 202.2 126.1 5.2 36 A ASP CA 181 203.5 126.6 5.4 34 A ASP CB 181 203.6 128.0 5.0 34 A ASP CG 181 204.9 128.6 5.0 35 A ASP OD1 181 205.9 127.9 5.2 35 A ASP OD2 181 205.1 129.9 4.9 36 A ASP C 181 203.9 126.5 6.9 35 A ASP O 181 203.4 127.3 7.7 37 A PRO N 182 204.7 125.5 7.3 35 A PRO CD 182 205.0 124.3 6.5 34 A PRO CA 182 205.1 125.3 8.7 35 A PRO CB 182 205.1 123.8 8.8 35 A PRO CG 182 205.8 123.5 7.5 35 A PRO C 182 206.4 125.9 8.9 35 A PRO O 182 207.0 125.6 10.0 34 A SER N 183 206.9 126.7 8.0 35 A SER CA 183 208.3 127.2 8.0 36 A SER CB 183 208.7 127.8 6.7 36 A SER OG 183 207.9 129.0 6.4 39 A SER C 183 208.7 128.2 9.1 35 A SER O 183 209.8 128.4 9.4 37 A GLN N 184 207.7 128.9 9.7 35 A GLN CA 184 208.0 129.9 10.8 34 A GLN CB 184 207.1 131.1 10.5 36 A GLN CG 184 207.3 131.8 9.2 40 A GLN CD 184 206.0 132.5 8.7 42 A GLN OE1 184 205.7 133.6 9.2 42 A GLN NE2 184 205.2 131.9 7.8 42 A GLN C 184 207.6 129.3 12.2 31 A GLN O 184 208.1 129.9 13.2 29 A GLU N 185 206.9 128.2 12.2 28 A GLU CA 185 206.5 127.6 13.4 27 A GLU CB 185 205.6 126.4 13.1 28 A GLU CG 185 204.4 126.7 12.2 28 A GLU CD 185 203.7 128.0 12.6 29 A GLU OE1 185 202.7 127.9 13.5 31 A GLU OE2 185 204.0 129.1 12.1 30 A GLU C 185 207.4 127.2 14.6 27 A GLU O 185 207.2 127.7 15.6 27 A LEU N 186 208.3 126.3 14.3 27 A LEU CA 186 209.2 125.9 15.4 28 A LEU CB 186 210.2 124.8 14.9 27 A LEU CG 186 209.4 123.5 14.4 26 A LEU CD1 186 210.4 122.4 14.1 27 A LEU CD2 186 208.4 123.1 15.4 26 A LEU C 186 210.0 127.1 16.0 29 A LEU O 186 210.3 127.1 17.2 29 A GLU N 187 210.3 128.1 15.2 31 A GLU CA 187 211.0 129.3 15.6 32 A GLU CB 187 211.6 130.0 14.4 36 A GLU CG 187 212.5 131.2 14.7 41 A GLU CD 187 213.0 132.0 13.4 45 A GLU OE1 187 213.1 131.3 12.3 46 A GLU OE2 187 213.3 133.2 13.5 47 A GLU C 187 210.1 130.2 16.4 30 A GLU O 187 210.6 130.9 17.3 31 A PHE N 188 208.9 130.3 16.0 27 A PHE CA 188 207.9 131.2 16.7 24 A PHE CB 188 206.6 131.3 16.0 23 A PHE CG 188 205.6 131.9 16.8 23 A PHE CD1 188 205.7 133.1 17.4 23 A PHE CD2 188 204.4 131.2 17.1 23 A PHE CE1 188 204.7 133.7 18.2 24 A PHE CE2 188 203.4 131.7 17.9 23 A PHE CZ 188 203.6 133.0 18.5 24 A PHE C 188 207.7 130.6 18.1 24 A PHE O 188 207.8 131.2 19.1 24 A ILE N 189 207.3 129.3 18.1 23 A ILE CA 189 207.0 128.5 19.3 21 A ILE CB 189 206.8 127.0 19.0 19 A ILE CG2 189 206.5 126.3 20.2 20 A ILE CG1 189 205.6 126.9 18.1 17 A ILE CD1 189 205.4 125.5 17.6 19 A ILE C 189 208.2 128.6 20.3 22 A ILE O 189 208.0 129.1 21.4 22 A ALA N 190 209.4 128.3 19.8 21 A ALA CA 190 210.6 128.4 20.7 20 A ALA CB 190 211.8 128.0 19.9 18 A ALA C 190 210.7 129.8 21.3 21 A ALA O 190 211.3 129.9 22.4 24 A ASP N 191 210.2 130.8 20.6 23 A ASP CA 191 210.3 132.2 21.2 24 A ASP CB 191 210.1 133.3 20.2 25 A ASP CG 191 210.1 134.6 20.9 28 A ASP OD1 191 211.2 135.0 21.3 29 A ASP OD2 191 209.0 135.3 21.0 30 A ASP C 191 209.3 132.3 22.3 24 A ASP O 191 209.5 133.0 23.4 23 A ILE N 192 208.1 131.7 22.2 23 A ILE CA 192 207.1 131.7 23.2 22 A ILE CB 192 205.7 131.2 22.7 20 A ILE CG2 192 204.7 131.1 23.8 20 A ILE CG1 192 205.2 132.1 21.6 19 A ILE CD1 192 204.8 133.5 22.1 18 A ILE C 192 207.6 130.8 24.4 23 A ILE O 192 207.5 131.2 25.5 24 A LEU N 193 208.1 129.7 24.1 24 A LEU CA 193 208.6 128.8 25.1 25 A LEU CB 193 209.0 127.4 24.5 24 A LEU CG 193 207.8 126.6 24.0 23 A LEU CD1 193 208.3 125.3 23.4 22 A LEU CD2 193 206.9 126.2 25.1 24 A LEU C 193 209.9 129.4 25.8 27 A LEU O 193 210.4 128.8 26.7 28 A ASN N 194 210.4 130.5 25.2 30 A ASN CA 194 211.6 131.1 25.8 31 A ASN CB 194 212.3 131.9 24.7 34 A ASN CG 194 213.7 132.4 25.2 37 A ASN OD1 194 213.9 133.6 25.1 38 A ASN ND2 194 214.5 131.4 25.7 37 A ASN C 194 211.1 132.1 26.9 31 A ASN O 194 211.8 132.4 27.8 30 A GLN N 195 209.8 132.5 26.8 29 A GLN CA 195 209.2 133.4 27.7 27 A GLN CB 195 208.2 134.3 27.0 28 A GLN CG 195 208.9 135.3 26.1 29 A GLN CD 195 208.1 135.8 25.0 29 A GLN OE1 195 207.2 136.6 25.1 31 A GLN NE2 195 208.4 135.3 23.8 30 A GLN C 195 208.5 132.5 28.8 26 A GLN O 195 208.4 133.0 30.0 28 A ASP N 196 208.1 131.3 28.5 24 A ASP CA 196 207.4 130.5 29.4 22 A ASP CB 196 205.9 130.8 29.4 22 A ASP CG 196 205.1 129.9 30.3 23 A ASP OD1 196 205.6 129.0 30.9 25 A ASP OD2 196 203.9 130.2 30.5 23 A ASP C 196 207.6 129.0 28.9 21 A ASP O 196 206.8 128.5 28.1 21 A ALA N 197 208.6 128.4 29.4 20 A ALA CA 197 209.0 127.1 29.0 21 A ALA CB 197 210.3 126.7 29.6 21 A ALA C 197 208.0 125.9 29.1 21 A ALA O 197 208.2 124.8 28.8 23 A LYS N 198 206.8 126.3 29.6 21 A LYS CA 198 205.8 125.3 29.8 19 A LYS CB 198 205.6 125.0 31.3 20 A LYS CG 198 206.9 124.6 32.0 19 A LYS CD 198 206.8 124.4 33.5 19 A LYS CE 198 208.2 124.1 34.1 20 A LYS NZ 198 208.1 123.6 35.5 21 A LYS C 198 204.4 125.7 29.3 19 A LYS O 198 203.4 125.2 29.8 21 A ASN N 199 204.3 126.7 28.4 17 A ASN CA 199 203.1 127.1 27.9 17 A ASN CB 199 203.2 128.2 26.8 17 A ASN CG 199 201.9 128.8 26.4 18 A ASN OD1 199 201.1 128.2 25.6 18 A ASN ND2 199 201.5 130.0 26.9 17 A ASN C 199 202.5 125.8 27.2 18 A ASN O 199 203.1 125.2 26.4 22 A TYR N 200 201.3 125.3 27.8 19 A TYR CA 200 200.6 124.1 27.2 19 A TYR CB 200 199.4 123.8 28.1 19 A TYR CG 200 199.0 122.4 28.0 17 A TYR CD1 200 199.6 121.4 28.9 18 A TYR CE1 200 199.2 120.1 28.8 18 A TYR CD2 200 198.0 122.0 27.2 17 A TYR CE2 200 197.6 120.6 27.1 18 A TYR CZ 200 198.2 119.7 27.9 18 A TYR OH 200 197.7 118.4 27.9 17 A TYR C 200 200.2 124.3 25.8 20 A TYR O 200 200.4 123.4 25.0 21 A HIS N 201 199.7 125.4 25.5 21 A HIS CA 201 199.2 125.7 24.1 21 A HIS CB 201 198.5 127.1 24.1 21 A HIS CG 201 197.3 127.1 24.9 22 A HIS CD2 201 197.0 127.5 26.2 21 A HIS ND1 201 196.1 126.6 24.4 21 A HIS CE1 201 195.1 126.7 25.4 22 A HIS NE2 201 195.7 127.2 26.5 22 A HIS C 201 200.4 125.7 23.1 21 A HIS O 201 200.3 125.2 22.0 23 A ALA N 202 201.6 126.3 23.5 19 A ALA CA 202 202.8 126.3 22.7 19 A ALA CB 202 203.9 127.1 23.4 18 A ALA C 202 203.3 124.9 22.4 20 A ALA O 202 203.6 124.6 21.3 21 A TRP N 203 203.3 124.1 23.5 21 A TRP CA 203 203.8 122.7 23.3 22 A TRP CB 203 204.0 122.0 24.6 21 A TRP CG 203 205.2 122.3 25.2 20 A TRP CD2 203 206.5 122.0 24.8 19 A TRP CE2 203 207.5 122.6 25.7 19 A TRP CE3 203 207.0 121.3 23.7 19 A TRP CD1 203 205.4 123.1 26.4 20 A TRP NE1 203 206.7 123.2 26.6 20 A TRP CZ2 203 208.8 122.4 25.5 18 A TRP CZ3 203 208.4 121.1 23.5 18 A TRP CH2 203 209.3 121.7 24.4 18 A TRP C 203 202.8 121.8 22.4 23 A TRP O 203 203.3 121.0 21.6 22 A GLN N 204 201.5 122.1 22.6 22 A GLN CA 204 200.5 121.4 21.8 22 A GLN CB 204 199.1 121.7 22.4 22 A GLN CG 204 198.0 121.0 21.7 23 A GLN CD 204 196.7 121.2 22.3 24 A GLN OE1 204 195.7 121.3 21.7 25 A GLN NE2 204 196.7 121.2 23.7 24 A GLN C 204 200.6 121.8 20.4 23 A GLN O 204 200.4 120.9 19.5 23 A HIS N 205 200.7 123.1 20.1 23 A HIS CA 205 200.8 123.6 18.8 23 A HIS CB 205 200.8 125.1 18.8 22 A HIS CG 205 200.8 125.7 17.4 22 A HIS CD2 205 201.7 126.1 16.5 22 A HIS ND1 205 199.6 125.9 16.7 22 A HIS CE1 205 199.8 126.4 15.5 21 A HIS NE2 205 201.1 126.6 15.4 21 A HIS C 205 202.0 123.0 18.1 23 A HIS O 205 202.0 122.5 17.0 25 A ARG N 206 203.1 123.0 18.9 24 A ARG CA 206 204.4 122.4 18.4 24 A ARG CB 206 205.5 122.6 19.5 22 A ARG CG 206 206.8 122.6 19.0 22 A ARG CD 206 207.9 122.8 20.1 22 A ARG NE 206 209.2 122.6 19.6 22 A ARG CZ 206 210.0 123.6 19.0 24 A ARG NH1 206 209.5 124.8 18.9 24 A ARG NH2 206 211.2 123.3 18.5 24 A ARG C 206 204.3 121.0 18.0 25 A ARG O 206 204.7 120.7 16.9 25 A GLN N 207 203.6 120.2 18.8 24 A GLN CA 207 203.4 118.7 18.5 23 A GLN CB 207 202.8 118.0 19.6 20 A GLN CG 207 203.7 117.8 20.8 18 A GLN CD 207 203.1 116.9 21.8 18 A GLN OE1 207 201.9 116.4 21.7 16 A GLN NE2 207 203.8 116.5 22.8 16 A GLN C 207 202.6 118.6 17.2 23 A GLN O 207 202.8 117.6 16.5 25 A TRP N 208 201.7 119.5 16.9 24 A TRP CA 208 200.9 119.5 15.7 24 A TRP CB 208 199.7 120.4 15.8 22 A TRP CG 208 198.9 120.5 14.6 22 A TRP CD2 208 199.0 121.6 13.6 21 A TRP CE2 208 198.2 121.2 12.5 21 A TRP CE3 208 199.7 122.8 13.6 22 A TRP CD1 208 198.1 119.6 14.0 21 A TRP NE1 208 197.6 120.0 12.8 21 A TRP CZ2 208 198.0 122.0 11.4 21 A TRP CZ3 208 199.5 123.6 12.4 21 A TRP CH2 208 198.7 123.2 11.4 22 A TRP C 208 201.8 119.8 14.5 26 A TRP O 208 201.7 119.1 13.5 29 A VAL N 209 202.6 120.8 14.6 26 A VAL CA 209 203.4 121.2 13.5 25 A VAL CB 209 204.2 122.5 13.7 25 A VAL CG1 209 205.0 122.9 12.5 24 A VAL CG2 209 203.3 123.6 14.1 25 A VAL C 209 204.4 120.1 13.1 27 A VAL O 209 204.6 119.8 11.9 28 A ILE N 210 205.0 119.5 14.1 28 A ILE CA 210 205.9 118.4 13.9 28 A ILE CB 210 206.6 118.0 15.3 25 A ILE CG2 210 207.3 116.7 15.2 25 A ILE CG1 210 207.6 119.0 15.7 23 A ILE CD1 210 208.1 118.8 17.1 21 A ILE C 210 205.2 117.1 13.4 30 A ILE O 210 205.7 116.5 12.4 31 A GLN N 211 204.1 116.8 14.0 33 A GLN CA 211 203.4 115.6 13.5 37 A GLN CB 211 202.2 115.3 14.4 41 A GLN CG 211 202.0 113.9 14.8 47 A GLN CD 211 201.3 113.7 16.2 50 A GLN OE1 211 200.9 114.6 16.8 52 A GLN NE2 211 201.1 112.4 16.5 52 A GLN C 211 202.9 115.8 12.0 37 A GLN O 211 203.3 115.0 11.2 39 A GLU N 212 202.1 116.8 11.8 38 A GLU CA 212 201.5 117.0 10.5 39 A GLU CB 212 200.7 118.3 10.5 42 A GLU CG 212 199.4 118.2 11.2 48 A GLU CD 212 198.5 117.2 10.5 51 A GLU OE1 212 198.0 117.5 9.4 53 A GLU OE2 212 198.4 116.0 11.1 53 A GLU C 212 202.5 117.2 9.4 38 A GLU O 212 202.4 116.6 8.3 38 A PHE N 213 203.5 118.1 9.6 37 A PHE CA 213 204.5 118.4 8.6 36 A PHE CB 213 204.9 119.8 8.6 35 A PHE CG 213 203.8 120.7 8.3 36 A PHE CD1 213 202.9 121.1 9.2 37 A PHE CD2 213 203.6 121.1 7.0 36 A PHE CE1 213 201.8 121.9 8.9 37 A PHE CE2 213 202.5 121.9 6.6 37 A PHE CZ 213 201.6 122.3 7.6 37 A PHE C 213 205.7 117.5 8.7 37 A PHE O 213 206.7 117.7 7.9 37 A ARG N 214 205.7 116.5 9.6 38 A ARG CA 214 206.7 115.5 9.7 40 A ARG CB 214 206.8 114.6 8.5 43 A ARG CG 214 205.8 113.4 8.6 47 A ARG CD 214 205.0 113.1 7.3 51 A ARG NE 214 203.7 113.7 7.2 56 A ARG CZ 214 202.5 113.4 7.8 57 A ARG NH1 214 201.4 114.1 7.6 58 A ARG NH2 214 202.4 112.4 8.7 58 A ARG C 214 208.1 116.2 9.9 39 A ARG O 214 209.1 115.9 9.2 40 A LEU N 215 208.2 117.2 10.9 38 A LEU CA 215 209.4 117.9 11.2 37 A LEU CB 215 209.1 119.4 11.3 37 A LEU CG 215 208.2 120.1 10.3 36 A LEU CD1 215 208.0 121.5 10.6 36 A LEU CD2 215 208.7 120.0 8.9 37 A LEU C 215 210.1 117.4 12.4 38 A LEU O 215 210.5 118.2 13.3 38 A TRP N 216 210.4 116.1 12.4 37 A TRP CA 216 211.1 115.5 13.6 37 A TRP CB 216 210.7 114.0 13.6 33 A TRP CG 216 209.3 113.7 13.4 30 A TRP CD2 216 208.4 113.5 14.5 28 A TRP CE2 216 207.1 113.2 13.9 28 A TRP CE3 216 208.4 113.6 15.9 27 A TRP CD1 216 208.6 113.4 12.3 29 A TRP NE1 216 207.3 113.1 12.5 27 A TRP CZ2 216 206.0 113.0 14.7 27 A TRP CZ3 216 207.3 113.4 16.6 26 A TRP CH2 216 206.1 113.1 16.0 26 A TRP C 216 212.6 115.5 13.8 39 A TRP O 216 213.1 115.4 14.9 39 A ASP N 217 213.3 115.7 12.7 42 A ASP CA 217 214.8 115.7 12.8 45 A ASP CB 217 215.4 116.0 11.4 47 A ASP CG 217 214.8 115.0 10.3 50 A ASP OD1 217 214.7 115.4 9.2 51 A ASP OD2 217 214.5 113.8 10.7 51 A ASP C 217 215.6 116.4 13.8 45 A ASP O 217 216.5 115.8 14.4 47 A ASN N 218 215.2 117.6 14.2 45 A ASN CA 218 216.0 118.4 15.1 44 A ASN CB 218 216.5 119.7 14.6 47 A ASN CG 218 217.2 119.5 13.3 48 A ASN OD1 218 216.6 119.7 12.2 49 A ASN ND2 218 218.5 119.3 13.3 49 A ASN C 218 215.3 118.6 16.5 43 A ASN O 218 215.8 119.4 17.3 43 A GLU N 219 214.2 118.0 16.7 41 A GLU CA 219 213.4 118.2 18.0 40 A GLU CB 219 212.0 117.7 17.8 39 A GLU CG 219 211.1 118.1 19.0 37 A GLU CD 219 211.0 119.6 19.3 37 A GLU OE1 219 211.6 120.4 18.6 37 A GLU OE2 219 210.3 119.9 20.3 37 A GLU C 219 214.1 117.5 19.2 40 A GLU O 219 213.9 118.1 20.3 40 A LEU N 220 214.7 116.4 19.1 38 A LEU CA 220 215.3 115.8 20.2 36 A LEU CB 220 215.8 114.4 19.9 35 A LEU CG 220 216.2 113.7 21.2 35 A LEU CD1 220 215.2 113.8 22.3 34 A LEU CD2 220 216.6 112.3 20.9 36 A LEU C 220 216.5 116.7 20.7 37 A LEU O 220 216.8 116.7 21.9 36 A GLN N 221 217.1 117.3 19.7 39 A GLN CA 221 218.3 118.2 20.1 41 A GLN CB 221 219.0 118.7 18.8 46 A GLN CG 221 219.8 117.7 18.0 51 A GLN CD 221 219.2 117.1 16.7 55 A GLN OE1 221 219.6 117.4 15.6 55 A GLN NE2 221 218.1 116.3 16.9 55 A GLN C 221 217.7 119.4 20.8 40 A GLN O 221 218.5 120.0 21.7 41 A TYR N 222 216.5 119.8 20.5 38 A TYR CA 222 215.8 121.0 21.2 35 A TYR CB 222 214.6 121.3 20.4 33 A TYR CG 222 213.8 122.5 21.0 32 A TYR CD1 222 214.4 123.7 21.1 30 A TYR CE1 222 213.7 124.8 21.6 31 A TYR CD2 222 212.5 122.3 21.4 31 A TYR CE2 222 211.8 123.4 21.8 31 A TYR CZ 222 212.4 124.7 21.9 31 A TYR OH 222 211.7 125.8 22.4 32 A TYR C 222 215.5 120.6 22.6 36 A TYR O 222 215.6 121.4 23.5 35 A VAL N 223 214.9 119.4 22.7 36 A VAL CA 223 214.5 118.8 24.0 35 A VAL CB 223 213.9 117.4 23.8 34 A VAL CG1 223 213.8 116.7 25.1 34 A VAL CG2 223 212.5 117.5 23.2 34 A VAL C 223 215.7 118.8 24.9 36 A VAL O 223 215.6 119.2 26.1 37 A ASP N 224 216.8 118.3 24.4 37 A ASP CA 224 218.0 118.2 25.2 38 A ASP CB 224 219.1 117.5 24.4 39 A ASP CG 224 219.0 116.0 24.3 40 A ASP OD1 224 218.7 115.4 25.3 42 A ASP OD2 224 219.2 115.5 23.2 41 A ASP C 224 218.4 119.6 25.7 39 A ASP O 224 218.9 119.8 26.8 40 A GLN N 225 218.3 120.6 24.8 38 A GLN CA 225 218.7 122.0 25.1 37 A GLN CB 225 218.4 122.8 23.9 39 A GLN CG 225 218.7 124.3 24.1 44 A GLN CD 225 218.2 125.2 22.9 47 A GLN OE1 225 218.2 124.8 21.7 50 A GLN NE2 225 217.8 126.5 23.2 48 A GLN C 225 217.8 122.5 26.3 35 A GLN O 225 218.4 122.9 27.3 34 A LEU N 226 216.5 122.3 26.2 32 A LEU CA 226 215.6 122.8 27.2 30 A LEU CB 226 214.2 122.7 26.8 28 A LEU CG 226 213.7 123.6 25.6 27 A LEU CD1 226 212.3 123.7 25.7 27 A LEU CD2 226 214.4 124.9 25.7 26 A LEU C 226 215.8 122.0 28.5 30 A LEU O 226 215.6 122.5 29.6 31 A LEU N 227 216.1 120.7 28.4 32 A LEU CA 227 216.4 119.9 29.6 34 A LEU CB 227 216.4 118.4 29.3 33 A LEU CG 227 215.0 117.7 29.3 34 A LEU CD1 227 215.1 116.3 28.8 34 A LEU CD2 227 214.4 117.8 30.6 33 A LEU C 227 217.6 120.3 30.3 36 A LEU O 227 217.8 120.1 31.5 35 A LYS N 228 218.5 121.0 29.6 38 A LYS CA 228 219.7 121.5 30.1 39 A LYS CB 228 220.7 121.9 29.0 41 A LYS CG 228 222.2 121.5 29.5 46 A LYS CD 228 223.1 122.8 29.4 49 A LYS CE 228 224.5 122.5 29.9 51 A LYS NZ 228 225.5 123.5 29.7 52 A LYS C 228 219.4 122.8 30.9 39 A LYS O 228 219.9 123.1 32.0 39 A GLU N 229 218.4 123.5 30.4 37 A GLU CA 229 218.0 124.8 31.1 36 A GLU CB 229 217.2 125.6 30.1 36 A GLU CG 229 218.0 126.1 28.9 35 A GLU CD 229 217.3 126.8 27.8 36 A GLU OE1 229 216.0 126.9 27.9 38 A GLU OE2 229 217.9 127.2 26.8 37 A GLU C 229 217.1 124.5 32.4 35 A GLU O 229 217.3 125.2 33.3 35 A ASP N 230 216.3 123.5 32.4 34 A ASP CA 230 215.5 123.2 33.5 32 A ASP CB 230 214.2 124.0 33.6 31 A ASP CG 230 213.5 123.9 34.9 31 A ASP OD1 230 213.8 123.0 35.7 30 A ASP OD2 230 212.7 124.8 35.2 31 A ASP C 230 215.2 121.7 33.4 32 A ASP O 230 214.2 121.3 32.8 32 A VAL N 231 216.0 120.9 34.1 31 A VAL CA 231 215.8 119.4 34.1 31 A VAL CB 231 217.0 118.7 34.7 32 A VAL CG1 231 217.0 118.9 36.2 33 A VAL CG2 231 216.9 117.2 34.4 32 A VAL C 231 214.5 119.0 34.7 30 A VAL O 231 214.1 117.9 34.6 31 A ARG N 232 213.9 120.0 35.4 30 A ARG CA 232 212.6 119.7 36.1 29 A ARG CB 232 212.5 120.4 37.4 30 A ARG CG 232 213.5 120.1 38.4 31 A ARG CD 232 213.2 120.9 39.7 32 A ARG NE 232 214.1 120.7 40.8 32 A ARG CZ 232 215.3 121.1 40.9 33 A ARG NH1 232 215.9 121.9 39.9 33 A ARG NH2 232 216.1 120.8 41.9 34 A ARG C 232 211.4 120.1 35.1 28 A ARG O 232 210.3 120.1 35.6 27 A ASN N 233 211.7 120.4 33.9 28 A ASN CA 233 210.7 120.8 33.0 27 A ASN CB 233 211.2 121.6 31.8 26 A ASN CG 233 210.1 122.4 31.1 26 A ASN OD1 233 208.9 121.9 31.0 26 A ASN ND2 233 210.4 123.5 30.4 24 A ASN C 233 209.9 119.6 32.4 27 A ASN O 233 210.3 119.1 31.3 29 A ASN N 234 208.8 119.2 33.1 27 A ASN CA 234 208.0 118.1 32.7 26 A ASN CB 234 206.8 117.9 33.7 26 A ASN CG 234 206.3 116.5 33.7 27 A ASN OD1 234 207.0 115.6 34.1 27 A ASN ND2 234 205.0 116.3 33.3 24 A ASN C 234 207.5 118.1 31.2 26 A ASN O 234 207.2 117.1 30.6 26 A SER N 235 207.3 119.3 30.7 26 A SER CA 235 206.8 119.5 29.3 26 A SER CB 235 206.5 121.0 29.1 24 A SER OG 235 205.4 121.4 29.9 22 A SER C 235 207.9 119.0 28.3 26 A SER O 235 207.5 118.5 27.3 27 A VAL N 236 209.1 119.1 28.7 26 A VAL CA 236 210.2 118.7 27.9 25 A VAL CB 236 211.5 119.4 28.3 25 A VAL CG1 236 212.6 119.1 27.3 26 A VAL CG2 236 211.2 120.9 28.3 24 A VAL C 236 210.4 117.2 28.1 25 A VAL O 236 210.7 116.5 27.1 25 A TRP N 237 210.2 116.6 29.3 25 A TRP CA 237 210.3 115.2 29.5 26 A TRP CB 237 210.2 114.8 30.9 27 A TRP CG 237 211.5 115.0 31.7 28 A TRP CD2 237 212.6 114.2 31.6 28 A TRP CE2 237 213.6 114.7 32.5 29 A TRP CE3 237 213.0 113.0 30.9 28 A TRP CD1 237 211.8 116.0 32.6 28 A TRP NE1 237 213.0 115.8 33.1 29 A TRP CZ2 237 214.9 114.2 32.7 27 A TRP CZ3 237 214.2 112.4 31.1 26 A TRP CH2 237 215.2 113.0 32.0 26 A TRP C 237 209.3 114.5 28.6 26 A TRP O 237 209.5 113.6 27.9 26 A ASN N 238 208.1 115.1 28.6 27 A ASN CA 238 207.0 114.6 27.9 28 A ASN CB 238 205.7 115.4 28.1 29 A ASN CG 238 204.5 114.9 27.3 31 A ASN OD1 238 203.9 113.8 27.7 31 A ASN ND2 238 204.1 115.5 26.2 30 A ASN C 238 207.3 114.7 26.4 28 A ASN O 238 207.1 113.8 25.6 28 A GLN N 239 207.9 115.8 25.9 28 A GLN CA 239 208.3 116.1 24.5 29 A GLN CB 239 208.8 117.5 24.3 28 A GLN CG 239 209.0 117.8 22.9 28 A GLN CD 239 207.7 118.1 22.1 28 A GLN OE1 239 206.6 117.8 22.6 30 A GLN NE2 239 207.8 118.5 20.9 28 A GLN C 239 209.3 115.1 24.0 29 A GLN O 239 209.3 114.7 22.9 29 A ARG N 240 210.2 114.7 24.9 29 A ARG CA 240 211.3 113.7 24.6 28 A ARG CB 240 212.2 113.7 25.8 28 A ARG CG 240 213.3 112.7 25.7 28 A ARG CD 240 214.2 112.5 27.0 26 A ARG NE 240 215.4 111.9 26.5 27 A ARG CZ 240 216.4 112.5 26.0 29 A ARG NH1 240 216.4 113.9 25.8 29 A ARG NH2 240 217.4 111.8 25.4 30 A ARG C 240 210.6 112.4 24.4 29 A ARG O 240 211.1 111.6 23.6 31 A HIS N 241 209.5 112.1 25.1 29 A HIS CA 241 208.9 110.8 24.9 27 A HIS CB 241 207.9 110.6 26.1 28 A HIS CG 241 207.3 109.2 26.1 30 A HIS CD2 241 207.5 108.2 27.0 30 A HIS ND1 241 206.5 108.7 25.1 30 A HIS CE1 241 206.2 107.4 25.4 30 A HIS NE2 241 206.9 107.1 26.5 30 A HIS C 241 208.1 110.9 23.6 28 A HIS O 241 208.1 109.9 22.8 29 A PHE N 242 207.4 112.0 23.4 28 A PHE CA 242 206.7 112.2 22.1 27 A PHE CB 242 206.1 113.6 22.1 24 A PHE CG 242 205.5 114.1 20.8 23 A PHE CD1 242 204.2 113.7 20.4 22 A PHE CD2 242 206.2 114.9 19.9 23 A PHE CE1 242 203.6 114.2 19.3 21 A PHE CE2 242 205.6 115.4 18.8 22 A PHE CZ 242 204.3 115.0 18.4 21 A PHE C 242 207.5 112.0 20.9 28 A PHE O 242 207.2 111.2 20.0 30 A VAL N 243 208.7 112.6 21.0 29 A VAL CA 243 209.7 112.5 19.9 31 A VAL CB 243 210.8 113.5 20.1 30 A VAL CG1 243 211.8 113.3 19.0 31 A VAL CG2 243 210.2 114.9 20.1 30 A VAL C 243 210.2 111.1 19.7 31 A VAL O 243 210.1 110.5 18.6 33 A ILE N 244 210.9 110.5 20.7 31 A ILE CA 244 211.5 109.2 20.6 31 A ILE CB 244 212.2 108.8 21.8 29 A ILE CG2 244 212.6 107.3 21.7 30 A ILE CG1 244 213.4 109.6 22.1 28 A ILE CD1 244 213.9 109.5 23.5 25 A ILE C 244 210.4 108.2 20.2 32 A ILE O 244 210.6 107.4 19.2 33 A SER N 245 209.3 108.1 20.9 33 A SER CA 245 208.3 107.2 20.6 34 A SER CB 245 207.2 107.1 21.7 34 A SER OG 245 206.3 108.2 21.5 35 A SER C 245 207.7 107.3 19.2 36 A SER O 245 207.1 106.3 18.8 39 A ASN N 246 207.8 108.4 18.6 37 A ASN CA 246 207.3 108.6 17.2 38 A ASN CB 246 206.5 109.9 17.1 36 A ASN CG 246 205.1 109.8 17.6 37 A ASN OD1 246 204.9 110.3 18.7 37 A ASN ND2 246 204.3 109.2 16.9 37 A ASN C 246 208.3 108.5 16.1 39 A ASN O 246 208.0 108.4 14.9 38 A THR N 247 209.6 108.5 16.5 40 A THR CA 247 210.6 108.3 15.5 41 A THR CB 247 211.7 109.4 15.8 40 A THR OG1 247 212.2 109.4 17.1 40 A THR CG2 247 211.1 110.8 15.5 39 A THR C 247 211.3 106.9 15.6 42 A THR O 247 211.1 106.2 14.7 43 A THR N 248 212.0 106.6 16.7 41 A THR CA 248 212.6 105.3 16.8 39 A THR CB 248 214.0 105.4 17.3 39 A THR OG1 248 214.0 105.7 18.7 39 A THR CG2 248 214.8 106.5 16.6 39 A THR C 248 211.9 104.3 17.6 40 A THR O 248 211.9 103.1 17.4 43 A GLY N 249 211.3 104.8 18.7 41 A GLY CA 249 210.6 103.9 19.6 40 A GLY C 249 211.6 103.5 20.7 41 A GLY O 249 212.8 103.8 20.5 40 A TYR N 250 211.1 102.9 21.7 42 A TYR CA 250 212.0 102.4 22.8 43 A TYR CB 250 211.3 102.8 24.2 41 A TYR CG 250 211.2 104.2 24.5 40 A TYR CD1 250 210.1 105.0 24.1 38 A TYR CE1 250 210.0 106.3 24.3 37 A TYR CD2 250 212.2 104.9 25.2 39 A TYR CE2 250 212.2 106.2 25.4 39 A TYR CZ 250 211.0 106.9 25.0 38 A TYR OH 250 211.0 108.3 25.3 38 A TYR C 250 212.2 100.9 22.8 46 A TYR O 250 212.8 100.4 23.8 47 A SER N 251 211.8 100.3 21.7 49 A SER CA 251 212.1 98.9 21.6 51 A SER CB 251 211.1 98.3 20.6 52 A SER OG 251 211.0 99.1 19.4 54 A SER C 251 213.5 98.6 21.2 52 A SER O 251 214.0 97.6 21.5 54 A ASP N 252 214.2 99.6 20.6 54 A ASP CA 252 215.6 99.5 20.2 54 A ASP CB 252 216.0 100.6 19.2 57 A ASP CG 252 217.4 100.4 18.6 59 A ASP OD1 252 218.2 99.6 19.2 60 A ASP OD2 252 217.6 101.0 17.5 61 A ASP C 252 216.5 99.5 21.4 54 A ASP O 252 216.6 100.5 22.1 53 A ARG N 253 217.1 98.3 21.7 54 A ARG CA 253 218.0 98.1 22.9 54 A ARG CB 253 218.8 96.8 22.7 56 A ARG CG 253 218.2 95.6 23.3 58 A ARG CD 253 219.0 94.3 23.0 60 A ARG NE 253 218.4 93.2 23.7 62 A ARG CZ 253 218.2 92.0 23.2 62 A ARG NH1 253 218.5 91.8 21.9 62 A ARG NH2 253 217.6 91.1 23.9 62 A ARG C 253 219.0 99.2 23.1 53 A ARG O 253 219.2 99.6 24.3 53 A ALA N 254 219.6 99.7 22.1 51 A ALA CA 254 220.6 100.8 22.2 49 A ALA CB 254 221.3 101.0 20.9 50 A ALA C 254 219.9 102.0 22.7 49 A ALA O 254 220.4 102.7 23.5 49 A VAL N 255 218.7 102.3 22.1 48 A VAL CA 255 217.9 103.5 22.4 46 A VAL CB 255 216.7 103.6 21.5 47 A VAL CG1 255 215.9 104.9 21.8 47 A VAL CG2 255 217.2 103.8 20.0 46 A VAL C 255 217.4 103.4 23.8 45 A VAL O 255 217.6 104.3 24.6 46 A LEU N 256 216.8 102.2 24.2 44 A LEU CA 256 216.3 102.0 25.5 44 A LEU CB 256 215.8 100.6 25.6 42 A LEU CG 256 215.2 100.1 27.0 41 A LEU CD1 256 214.2 101.1 27.5 41 A LEU CD2 256 214.5 98.8 26.7 42 A LEU C 256 217.5 102.3 26.5 46 A LEU O 256 217.4 103.1 27.4 46 A GLU N 257 218.6 101.6 26.3 48 A GLU CA 257 219.8 101.7 27.2 49 A GLU CB 257 220.9 100.9 26.6 51 A GLU CG 257 222.3 101.3 27.1 56 A GLU CD 257 222.6 101.0 28.5 59 A GLU OE1 257 221.8 100.3 29.2 60 A GLU OE2 257 223.6 101.5 29.1 59 A GLU C 257 220.2 103.2 27.3 48 A GLU O 257 220.5 103.7 28.4 48 A ARG N 258 220.4 103.9 26.2 48 A ARG CA 258 220.8 105.3 26.1 48 A ARG CB 258 220.8 105.8 24.7 47 A ARG CG 258 221.1 107.3 24.6 46 A ARG CD 258 220.6 107.9 23.3 46 A ARG NE 258 219.2 108.0 23.2 47 A ARG CZ 258 218.4 108.0 22.1 46 A ARG NH1 258 219.0 108.1 20.9 47 A ARG NH2 258 217.1 108.0 22.1 47 A ARG C 258 219.9 106.1 27.0 48 A ARG O 258 220.3 106.9 27.8 50 A GLU N 259 218.6 105.8 26.9 47 A GLU CA 259 217.6 106.5 27.7 45 A GLU CB 259 216.1 106.2 27.1 44 A GLU CG 259 215.8 106.8 25.8 43 A GLU CD 259 216.0 108.3 25.8 43 A GLU OE1 259 215.5 109.0 26.6 43 A GLU OE2 259 216.7 108.8 24.9 41 A GLU C 259 217.6 106.3 29.2 44 A GLU O 259 217.7 107.2 29.9 44 A VAL N 260 217.6 105.0 29.6 44 A VAL CA 260 217.7 104.7 31.0 43 A VAL CB 260 247.6 103.1 31.2 42 A VAL CG1 260 217.8 102.8 32.7 40 A VAL CG2 260 216.2 102.6 30.7 41 A VAL C 260 219.0 105.2 31.6 44 A VAL O 260 218.9 105.6 32.8 44 A GLN N 261 220.0 105.2 30.9 45 A GLN CA 261 221.3 105.6 31.3 47 A GLN CB 261 222.4 105.4 30.3 49 A GLN CG 261 223.8 105.3 30.8 54 A GLN CD 261 223.9 104.2 31.9 56 A GLN OE1 261 223.8 103.1 31.5 58 A GLN NE2 261 224.0 104.6 33.1 57 A GLN C 261 221.3 107.1 31.6 47 A GLN O 261 221.6 107.6 32.7 48 A TYR N 262 220.8 107.9 30.6 46 A TYR CA 262 220.6 109.3 30.7 44 A TYR CB 262 220.0 109.8 29.4 42 A TYR CG 262 219.5 111.3 29.5 41 A TYR CD1 262 220.4 112.3 29.5 41 A TYR CE1 262 220.0 113.6 29.7 41 A TYR CD2 262 218.2 111.5 29.6 40 A TYR CE2 262 217.7 112.8 29.8 39 A TYR CZ 262 218.6 113.8 29.8 40 A TYR OH 262 218.2 115.1 30.0 41 A TYR C 262 219.7 109.7 31.9 45 A TYR O 262 220.0 110.6 32.6 45 A THR N 263 218.6 108.9 32.0 44 A THR CA 263 217.6 109.2 33.0 44 A THR CB 263 216.3 108.5 32.7 43 A THR OG1 263 215.9 108.8 31.4 44 A THR CG2 263 215.2 109.1 33.6 42 A THR C 263 218.2 108.8 34.4 45 A THR O 263 217.9 109.5 35.4 45 A LEU N 264 218.9 107.8 34.5 46 A LEU CA 264 219.5 107.4 35.7 47 A LEU CB 264 220.1 106.0 35.7 45 A LEU CG 264 219.0 104.9 35.9 45 A LEU CD1 264 219.6 103.5 35.6 45 A LEU CD2 264 218.4 105.0 37.3 44 A LEU C 264 220.5 108.4 36.1 48 A LEU O 264 220.7 108.7 37.3 49 A GLU N 265 221.1 109.1 35.1 50 A GLU CA 265 222.0 110.2 35.4 53 A GLU CB 265 222.6 110.7 34.1 56 A GLU CG 265 224.1 110.3 33.9 61 A GLU CD 265 224.3 108.9 33.6 64 A GLU OE1 265 224.2 108.6 32.3 66 A GLU OE2 265 224.6 108.0 34.5 66 A GLU C 265 221.3 111.4 36.0 52 A GLU O 265 221.6 111.8 37.1 52 A MET N 266 220.2 111.9 35.3 51 A MET CA 266 219.4 113.0 35.8 50 A MET CB 266 218.3 113.4 34.9 50 A MET CG 266 218.7 113.7 33.4 50 A MET SD 266 220.3 114.5 33.3 52 A MET CE 266 220.0 116.1 34.0 52 A MET C 266 218.9 112.8 37.2 49 A MET O 266 218.5 113.7 37.9 49 A ILE N 267 218.7 111.5 37.5 50 A ILE CA 267 218.2 111.1 38.8 51 A ILE CB 267 217.7 109.6 38.8 50 A ILE CG2 267 217.5 109.1 40.2 49 A ILE CG1 267 216.3 109.6 38.1 49 A ILE CD1 267 215.7 108.2 38.0 48 A ILE C 267 219.4 111.1 39.8 54 A ILE O 267 219.2 111.7 40.9 55 A LYS N 268 220.5 110.6 39.4 55 A LYS CA 268 221.7 110.6 40.3 56 A LYS CB 268 222.6 109.4 39.9 59 A LYS CG 268 221.9 108.0 40.0 61 A LYS CD 268 222.8 106.9 39.4 63 A LYS CE 268 222.0 105.5 39.4 64 A LYS NZ 268 222.9 104.3 39.0 65 A LYS C 268 222.4 111.9 40.0 55 A LYS O 268 223.6 111.9 39.7 57 A LEU N 269 221.6 113.0 40.1 52 A LEU CA 269 222.1 114.4 39.9 50 A LEU CB 269 222.2 114.7 38.4 50 A LEU CG 269 222.9 115.9 37.8 51 A LEU CD1 269 221.9 116.9 37.2 51 A LEU CD2 269 223.7 116.6 38.9 52 A LEU C 269 221.1 115.3 40.6 48 A LEU O 269 221.5 116.3 41.2 49 A VAL N 270 219.8 115.0 40.4 46 A VAL CA 270 218.7 115.8 41.1 44 A VAL CB 270 218.0 116.8 40.1 41 A VAL CG1 270 217.1 117.7 40.9 39 A VAL CG2 270 219.1 117.6 39.4 40 A VAL C 270 217.7 114.7 41.6 45 A VAL O 270 216.5 114.8 41.2 45 A PRO N 271 218.1 113.8 42.5 43 A PRO CD 271 219.4 113.8 43.2 43 A PRO CA 271 217.3 112.7 43.0 42 A PRO CB 271 218.2 112.2 44.2 42 A PRO CG 271 219.1 113.3 44.5 42 A PRO C 271 215.9 113.1 43.5 41 A PRO O 271 215.1 112.2 43.5 42 A HIS N 272 215.6 114.3 43.8 40 A HIS CA 272 214.3 114.7 44.2 41 A HIS CB 272 214.3 115.6 45.4 42 A HIS CG 272 214.6 114.8 46.7 42 A HIS CD2 272 213.7 114.2 47.6 42 A HIS ND1 272 215.9 114.6 47.1 41 A HIS CE1 272 215.8 113.9 48.2 42 A HIS NE2 272 214.5 113.7 48.5 42 A HIS C 272 213.4 115.3 43.1 41 A HIS O 272 212.3 115.8 43.3 43 A ASN N 273 213.9 115.3 41.8 39 A ASN CA 273 213.2 115.8 40.7 36 A ASN CB 273 214.2 116.1 39.6 34 A ASN CG 273 213.6 116.4 38.2 33 A ASN OD1 273 212.4 116.7 38.2 32 A ASN ND2 273 214.4 116.2 37.2 33 A ASN C 273 212.3 114.6 40.2 36 A ASN O 273 212.8 113.6 39.7 36 A GLU N 274 211.0 114.8 40.4 35 A GLU CA 274 210.1 113.8 40.0 34 A GLU CB 274 208.7 114.2 40.5 34 A GLU CG 274 207.7 113.1 40.3 37 A GLU CD 274 206.4 113.5 40.8 38 A GLU OE1 274 205.4 113.1 40.2 39 A GLU OE2 274 206.4 114.4 41.7 41 A GLU C 274 210.0 113.4 38.6 35 A GLU O 274 209.8 112.2 38.3 36 A SER N 275 210.1 114.3 37.6 35 A SER CA 275 209.9 114.0 36.2 34 A SER CB 275 210.2 115.3 35.4 34 A SER OG 275 209.2 116.3 35.7 35 A SER C 275 210.8 112.9 35.7 34 A SER O 275 210.3 112.0 35.0 33 A ALA N 276 212.1 113.0 36.0 33 A ALA CA 276 213.1 111.9 35.6 33 A ALA CB 276 214.5 112.3 36.1 31 A ALA C 276 212.7 110.6 36.1 34 A ALA O 276 212.8 109.6 35.4 35 A TRP N 277 212.1 110.5 37.2 35 A TRP CA 277 211.6 109.3 37.8 35 A TRP CB 277 211.2 109.5 39.3 37 A TRP CG 277 212.4 109.4 40.2 39 A TRP CD2 277 213.1 108.2 40.5 40 A TRP CE2 277 214.2 108.6 41.3 40 A TRP CE3 277 213.0 106.9 40.2 40 A TRP CD1 277 213.0 110.4 40.8 40 A TRP NE1 277 214.1 109.9 41.5 41 A TRP CZ2 277 215.1 107.7 41.8 40 A TRP CZ3 277 213.9 105.9 40.7 39 A TRP CH2 277 214.9 106.3 41.5 39 A TRP C 277 210.4 108.7 37.1 35 A TRP O 277 210.3 107.5 36.8 34 A ASN N 278 209.4 109.6 36.8 35 A ASN CA 278 208.2 109.2 36.1 35 A ASN CB 278 207.1 110.4 36.1 37 A ASN CG 278 206.8 110.8 37.6 37 A ASN OD1 278 207.2 110.1 38.5 38 A ASN ND2 278 206.0 111.8 37.7 35 A ASN C 278 208.5 108.9 34.6 34 A ASN O 278 207.8 108.2 34.0 33 A TYR N 279 209.6 109.4 34.1 34 A TYR CA 279 210.1 109.1 32.8 35 A TYR CB 279 211.1 110.2 32.3 33 A TYR CG 279 211.5 109.9 30.9 31 A TYR CD1 279 210.8 110.2 29.8 30 A TYR CE1 279 211.2 109.9 28.5 30 A TYR CD2 279 212.8 109.3 30.6 31 A TYR CE2 279 213.2 109.0 29.3 30 A TYR CZ 279 212.4 109.3 28.3 30 A TYR OH 279 212.9 109.1 27.0 29 A TYR C 279 210.7 107.7 32.7 37 A TYR O 279 210.3 106.9 32.0 38 A LEU N 280 211.7 107.5 33.6 38 A LEU CA 280 212.4 106.2 33.7 38 A LEU CB 280 213.4 106.2 34.9 38 A LEU CG 280 213.9 104.8 35.2 36 A LEU CD1 280 215.0 104.5 34.2 36 A LEU CD2 280 214.5 104.9 36.6 37 A LEU C 280 211.4 105.0 33.9 39 A LEU O 280 211.5 104.0 33.4 38 A LYS N 281 210.4 105.3 34.8 40 A LYS CA 281 209.4 104.4 35.1 41 A LYS CB 281 208.5 104.9 36.2 41 A LYS CG 281 207.2 104.1 36.4 42 A LYS CD 281 206.7 104.2 37.8 45 A LYS CE 281 205.3 104.7 38.0 47 A LYS NZ 281 205.3 106.2 37.8 49 A LYS C 281 208.5 104.2 33.9 42 A LYS O 281 208.2 103.0 33.5 41 A GLY N 282 208.2 105.3 33.2 42 A GLY CA 282 207.4 105.2 32.0 42 A GLY C 282 208.0 104.5 30.9 43 A GLY O 282 207.2 103.8 30.2 45 A ILE N 283 209.3 104.6 30.6 44 A ILE CA 283 209.9 103.9 29.5 45 A ILE CB 283 211.2 104.7 29.0 44 A ILE CG2 283 210.9 106.1 28.7 45 A ILE CG1 283 212.2 104.6 30.1 43 A ILE CD1 283 213.6 105.1 29.7 42 A ILE C 283 210.1 102.5 29.7 48 A ILE O 283 210.3 101.7 28.7 49 A LEU N 284 210.2 102.0 31.0 50 A LEU CA 284 210.5 100.6 31.3 52 A LEU CB 284 211.5 100.5 32.5 50 A LEU CG 284 212.9 101.0 32.4 50 A LEU CD1 284 213.6 100.7 33.7 50 A LEU CD2 284 213.6 100.3 31.2 50 A LEU C 284 209.2 99.8 31.7 54 A LEU O 284 209.1 98.7 31.2 53 A GLN N 285 208.4 100.5 32.5 58 A GLN CA 285 207.1 99.9 32.9 62 A GLN CB 285 206.3 100.8 33.8 64 A GLN CG 285 205.4 101.8 33.1 67 A GLN CD 285 204.5 102.7 34.0 68 A GLN OE1 285 203.8 103.6 33.5 70 A GLN NE2 285 204.6 102.5 35.3 69 A GLN C 285 206.2 99.3 31.8 64 A GLN O 285 205.2 98.7 32.0 65 A ASP N 286 206.6 99.6 30.6 66 A ASP CA 286 205.9 99.1 29.4 68 A ASP CB 286 205.6 100.2 28.4 70 A ASP CG 286 204.3 100.0 27.7 72 A ASP OD1 286 203.3 100.0 28.3 73 A ASP OD2 286 204.4 99.7 26.4 73 A ASP C 286 206.7 98.0 28.8 68 A ASP O 286 207.1 98.1 27.6 69 A ARG N 287 207.0 97.0 29.7 67 A ARG CA 287 207.8 95.8 29.3 66 A ARG CB 287 209.1 96.1 28.5 68 A ARG CG 287 209.6 95.0 27.7 70 A ARG CD 287 210.6 94.1 28.5 72 A ARG NE 287 211.1 93.0 27.7 74 A ARG CZ 287 212.4 92.6 27.7 75 A ARG NH1 287 213.2 93.2 28.5 76 A ARG NH2 287 212.7 91.5 27.0 74 A ARG C 287 208.1 95.0 30.5 63 A ARG O 287 208.4 93.8 30.4 63 A GLY N 288 207.8 95.6 31.7 61 A GLY CA 288 208.0 94.9 32.9 59 A GLY C 288 209.3 95.3 33.6 58 A GLY O 288 210.4 95.1 33.0 59 A LEU N 289 209.2 96.0 34.7 56 A LEU CA 289 210.4 96.4 35.4 55 A LEU CB 289 210.0 97.2 36.7 52 A LEU CG 289 210.0 98.8 36.6 50 A LEU CD1 289 210.0 99.3 35.2 50 A LEU CD2 289 208.7 99.3 37.3 50 A LEU C 289 211.2 95.2 35.8 55 A LEU O 289 212.4 95.2 35.9 55 A SER N 290 210.5 94.1 36.1 55 A SER CA 290 211.1 92.9 36.5 56 A SER CB 290 210.1 91.9 37.2 56 A SER OG 290 209.2 91.5 36.3 58 A SER C 290 211.9 92.1 35.4 57 A SER O 290 212.6 91.2 35.7 57 A ARG N 291 211.8 92.6 34.2 57 A ARG CA 291 212.5 92.0 33.1 57 A ARG CB 291 211.8 92.1 31.7 59 A ARG CG 291 210.5 91.4 31.7 63 A ARG CD 291 209.8 91.4 30.3 66 A ARG NE 291 210.4 90.3 29.4 69 A ARG CZ 291 209.9 89.9 28.2 71 A ARG NH1 291 210.5 89.0 27.5 72 A ARG NH2 291 208.8 90.5 27.8 73 A ARG C 291 213.9 92.6 33.0 55 A ARG O 291 214.7 92.3 32.1 55 A TYR N 292 214.2 93.4 34.0 53 A TYR CA 292 215.4 94.2 34.2 51 A TYR CB 292 215.2 95.7 33.9 48 A TYR CG 292 214.6 95.9 32.6 45 A TYR CD1 292 213.3 96.3 32.4 44 A TYR CE1 292 212.7 96.5 31.2 44 A TYR CD2 292 215.3 95.7 31.5 44 A TYR CE2 292 214.8 95.8 30.2 45 A TYR CZ 292 213.5 96.2 30.0 45 A TYR OH 292 213.0 96.4 28.8 45 A TYR C 292 216.0 93.9 35.6 53 A TYR O 292 215.7 94.7 36.5 52 A PRO N 293 216.7 92.8 35.7 55 A PRO CD 293 217.2 92.0 34.6 55 A PRO CA 293 217.4 92.3 37.0 55 A PRO CB 293 218.1 91.1 36.5 55 A PRO CG 293 218.5 91.4 35.1 55 A PRO C 293 218.3 93.4 37.6 56 A PRO O 293 218.1 93.6 38.8 56 A ASN N 294 219.2 93.9 36.8 58 A ASN CA 294 220.1 94.9 37.3 60 A ASN CB 294 221.0 95.4 36.2 61 A ASN CG 294 221.8 94.3 35.5 61 A ASN OD1 294 221.3 93.7 34.5 62 A ASN ND2 294 223.0 94.0 35.9 61 A ASN C 294 219.4 96.1 37.9 61 A ASN O 294 219.9 96.7 38.9 61 A LEU N 295 218.2 96.4 37.4 63 A LEU CA 295 217.4 97.6 37.9 63 A LEU CB 295 216.0 97.5 37.3 63 A LEU CG 295 215.3 98.9 37.3 62 A LEU CD1 295 216.0 99.8 36.4 62 A LEU CD2 295 213.9 98.6 36.8 63 A LEU C 295 217.4 97.6 39.4 63 A LEU O 295 218.0 98.5 40.0 63 A LEU N 296 216.7 96.7 40.1 63 A LEU CA 296 216.5 96.7 41.5 64 A LEU CB 296 216.0 95.3 42.0 62 A LEU CG 296 215.8 95.2 43.5 61 A LEU CD1 296 214.8 96.3 44.0 60 A LEU CD2 296 215.3 93.8 43.9 61 A LEU C 296 217.9 97.0 42.3 65 A LEU O 296 217.9 97.6 43.3 65 A ASN N 297 219.0 96.5 41.7 67 A ASN CA 297 220.3 96.7 42.3 70 A ASN CB 297 221.3 95.8 41.7 72 A ASN CG 297 221.0 94.4 42.0 74 A ASN OD1 297 220.6 94.1 43.2 76 A ASN ND2 297 221.3 93.4 41.1 75 A ASN C 297 220.7 98.2 42.2 70 A ASN O 297 220.9 98.8 43.2 70 A GLN N 298 221.0 98.7 41.0 69 A GLN CA 298 221.4 100.0 40.8 69 A GLN CB 298 221.3 100.4 39.3 69 A GLN CG 298 221.3 99.3 38.3 70 A GLN CD 298 222.7 99.0 37.7 70 A GLN OE1 298 223.3 98.0 38.0 70 A GLN NE2 298 223.1 99.8 36.7 70 A GLN C 298 220.6 101.0 41.6 69 A GLN O 298 221.1 101.9 42.3 69 A LEU N 299 219.3 100.8 41.7 70 A LEU CA 299 218.4 101.6 42.4 72 A LEU CB 299 216.9 101.4 42.1 70 A LEU CG 299 216.4 101.7 40.7 69 A LEU CD1 299 214.9 101.8 40.8 68 A LEU CD2 299 216.9 103.0 40.2 69 A LEU C 299 218.6 101.5 43.9 73 A LEU O 299 218.5 102.4 44.7 74 A LEU N 300 218.9 100.2 44.3 75 A LEU CA 300 219.1 99.9 45.7 77 A LEU CB 300 219.2 98.4 45.9 76 A LEU CG 300 218.3 97.8 47.0 77 A LEU CD1 300 217.0 98.6 47.3 77 A LEU CD2 300 217.9 96.4 46.7 77 A LEU C 300 220.4 100.6 46.2 78 A LEU O 300 220.5 100.9 47.4 78 A ASP N 301 221.3 100.8 45.2 80 A ASP CA 301 222.6 101.4 45.5 83 A ASP CB 301 223.5 101.3 44.3 84 A ASP CG 301 223.9 99.8 44.0 86 A ASP OD1 301 223.7 98.9 44.9 87 A ASP OD2 301 224.5 99.5 42.9 86 A ASP C 301 222.4 102.9 45.9 84 A ASP O 301 223.1 103.4 46.7 85 A LEU N 302 221.4 103.5 45.3 84 A LEU CA 302 221.1 104.9 45.5 84 A LEU CB 302 220.2 105.4 44.4 85 A LEU CG 302 220.8 105.4 43.0 84 A LEU CD1 302 219.9 106.2 42.1 85 A LEU CD2 302 222.2 105.9 43.0 85 A LEU C 302 220.4 105.2 46.8 84 A LEU O 302 220.1 106.3 47.2 84 A GLN N 303 220.0 104.1 47.6 84 A GLN CA 303 219.3 104.2 48.9 85 A GLN CB 303 219.2 102.8 49.5 85 A GLN CG 303 217.9 102.1 49.1 86 A GLN CD 303 216.7 102.7 49.7 86 A GLN OE1 303 216.6 103.9 49.9 85 A GLN NE2 303 215.7 101.8 49.9 86 A GLN C 303 219.9 105.2 49.8 85 A GLN O 303 219.1 105.9 50.5 85 A PRO N 304 221.2 105.3 50.0 84 A PRO CD 304 222.2 104.2 49.7 84 A PRO CA 304 221.8 106.3 50.9 83 A PRO CB 304 222.8 105.4 51.7 83 A PRO CG 304 223.4 104.6 50.6 84 A PRO C 304 222.4 107.5 50.2 83 A PRO O 304 222.5 108.5 50.8 82 A SER N 305 222.8 107.3 49.0 83 A SER CA 305 223.5 108.4 48.2 82 A SER CB 305 224.5 107.8 47.3 83 A SER OG 305 225.7 107.3 48.0 83 A SER C 305 222.6 109.3 47.4 81 A SER O 305 222.9 110.4 47.0 81 A HIS N 306 221.4 108.8 47.0 79 A HIS CA 306 220.4 109.6 46.2 77 A HIS CB 306 220.7 109.4 44.7 78 A HIS CG 306 222.1 109.6 44.3 79 A HIS CD2 306 223.2 108.8 44.2 79 A HIS ND1 306 222.6 110.8 43.9 80 A HIS CE1 306 223.9 110.7 43.6 80 A HIS NE2 306 224.2 109.5 43.8 80 A HIS C 306 219.0 109.2 46.5 75 A HIS O 306 218.2 109.0 45.6 75 A SER N 307 218.6 109.2 47.8 72 A SER CA 307 217.2 108.8 48.2 69 A SER CB 307 217.3 107.9 49.4 70 A SER OG 307 216.1 107.1 49.6 70 A SER C 307 216.2 109.8 48.4 67 A SER O 307 216.4 110.9 48.9 66 A SER N 308 215.0 109.4 48.1 64 A SER CA 308 213.7 110.2 48.2 61 A SER CB 308 213.6 111.1 46.9 61 A SER OG 308 213.8 110.3 45.7 61 A SER C 308 212.6 109.2 48.2 59 A SER O 308 212.8 108.0 47.9 58 A PRO N 309 211.4 109.6 48.4 56 A PRO CD 309 210.9 111.0 48.9 56 A PRO CA 309 210.3 108.7 48.4 56 A PRO CB 309 209.1 109.5 49.0 57 A PRO CG 309 209.5 110.9 48.6 57 A PRO C 309 210.0 108.1 47.0 56 A PRO O 309 209.1 107.3 46.8 55 A TYR N 310 210.8 108.6 46.0 56 A TYR CA 310 210.7 108.2 44.6 55 A TYR CB 310 211.2 109.3 43.7 54 A TYR CG 310 210.7 110.6 43.9 53 A TYR CD1 310 211.5 111.7 44.2 53 A TYR CE1 310 210.9 113.0 44.5 53 A TYR CD2 310 209.3 110.8 43.8 53 A TYR CE2 310 208.7 112.1 44.1 53 A TYR CZ 310 209.6 113.1 44.4 53 A TYR OH 310 209.0 114.3 44.7 55 A TYR C 310 211.4 106.9 44.5 55 A TYR O 310 211.0 106.0 43.7 57 A LEU N 311 212.6 106.8 45.1 54 A LEU CA 311 213.4 105.6 45.1 53 A LEU CB 311 214.7 105.7 45.9 53 A LEU CG 311 215.8 104.7 45.8 54 A LEU CD1 311 216.2 104.5 44.3 55 A LEU CD2 311 217.0 105.0 46.6 54 A LEU C 311 212.6 104.5 45.7 51 A LEU O 311 212.4 103.4 45.1 51 A ILE N 312 212.0 104.8 46.9 51 A ILE CA 312 211.2 103.8 47.6 50 A ILE CB 312 210.7 104.4 49.0 50 A ILE CG2 312 209.9 103.5 49.8 50 A ILE CG1 312 212.0 104.9 49.8 51 A ILE CD1 312 211.6 105.6 51.1 52 A ILE C 312 209.9 103.5 46.8 49 A ILE O 312 209.4 102.3 46.9 48 A ALA N 313 209.3 104.5 46.2 46 A ALA CA 313 208.1 104.2 45.4 44 A ALA CB 313 207.4 105.5 45.0 45 A ALA C 313 208.4 103.4 44.1 43 A ALA O 313 207.6 102.5 43.7 42 A PHE N 314 209.6 103.6 43.6 42 A PHE CA 314 210.0 102.8 42.4 43 A PHE CB 314 211.3 103.4 41.7 43 A PHE CG 314 211.4 103.0 40.3 44 A PHE CD1 314 211.3 103.9 39.3 45 A PHE CD2 314 211.8 101.7 39.9 44 A PHE CE1 314 211.4 103.6 37.9 44 A PHE CE2 314 212.0 101.4 38.6 44 A PHE CZ 314 211.8 102.3 37.6 44 A PHE C 314 210.2 101.4 42.8 43 A PHE O 314 209.8 100.5 42.1 44 A LEU N 315 210.9 101.2 43.9 44 A LEU CA 315 211.2 99.9 44.4 42 A LEU CB 315 212.1 99.9 45.7 41 A LEU CG 315 213.5 100.6 45.6 40 A LEU CD1 315 214.1 100.7 47.0 39 A LEU CD2 315 214.4 99.8 44.7 40 A LEU C 315 209.9 99.2 44.6 42 A LEU O 315 209.7 98.0 44.3 42 A VAL N 316 208.9 99.9 45.2 42 A VAL CA 316 207.6 99.3 45.5 43 A VAL CB 316 206.7 100.2 46.2 43 A VAL CG1 316 205.4 99.5 46.5 42 A VAL CG2 316 207.3 100.6 47.5 44 A VAL C 316 207.0 98.9 44.2 45 A VAL O 316 206.2 98.0 44.1 45 A ASP N 317 207.4 99.5 43.1 47 A ASP CA 317 206.8 99.2 41.7 49 A ASP CB 317 206.9 100.4 40.8 51 A ASP CG 317 205.9 101.5 41.2 53 A ASP OD1 317 204.8 101.2 41.6 53 A ASP OD2 317 206.2 102.7 41.1 54 A ASP C 317 207.6 98.0 41.1 49 A ASP O 317 207.0 97.3 40.3 49 A ILE N 318 208.9 97.9 41.4 49 A ILE CA 318 209.6 96.8 40.8 49 A ILE CB 318 211.1 96.8 41.2 49 A ILE CG2 318 211.7 95.5 40.8 49 A ILE CG1 318 211.7 98.0 40.4 49 A ILE CD1 318 213.2 98.0 40.6 49 A ILE C 318 209.0 95.6 41.5 51 A ILE O 318 208.5 94.7 40.9 52 A TYR N 319 209.1 95.6 42.9 52 A TYR CA 319 208.6 94.5 43.7 54 A TYR CB 319 208.5 94.9 45.2 53 A TYR CG 319 209.9 95.0 45.8 52 A TYR CD1 319 210.1 95.9 46.9 52 A TYR CE1 319 211.4 96.0 47.5 51 A TYR CD2 319 211.0 94.3 45.3 51 A TYR CE2 319 212.3 94.5 45.9 51 A TYR CZ 319 212.4 95.4 46.9 51 A TYR OH 319 213.7 95.5 47.4 51 A TYR C 319 207.2 94.0 43.2 56 A TYR O 319 206.9 92.8 43.1 57 A GLU N 320 206.3 94.9 42.9 59 A GLU CA 320 204.9 94.6 42.4 62 A GLU CB 320 204.1 95.9 42.0 65 A GLU CG 320 203.7 96.7 43.2 68 A GLU CD 320 203.5 98.2 42.9 70 A GLU OE1 320 203.3 99.0 43.8 72 A GLU OE2 320 203.4 98.5 41.7 71 A GLU C 320 205.0 93.7 41.2 63 A GLU O 320 204.2 92.8 41.0 63 A ASP N 321 205.9 94.0 40.3 63 A ASP CA 321 206.1 93.3 39.0 64 A ASP CB 321 206.7 94.2 38.0 63 A ASP CG 321 206.6 93.6 36.6 63 A ASP OD1 321 205.5 93.1 36.2 64 A ASP OD2 321 207.6 93.5 35.8 63 A ASP C 321 206.8 92.0 39.2 65 A ASP O 321 206.7 91.1 38.3 65 A MET N 322 207.7 91.9 40.2 66 A MET CA 322 208.4 90.6 40.4 69 A MET CB 322 209.6 90.8 41.3 68 A MET CG 322 210.6 91.8 40.8 68 A MET SD 322 212.1 91.6 41.8 69 A MET CE 322 211.5 91.8 43.4 68 A MET C 322 207.4 89.7 41.0 71 A MET O 322 207.7 88.5 41.1 73 A LEU N 323 206.3 90.2 41.5 74 A LEU CA 323 205.3 89.4 42.1 76 A LEU CB 323 204.6 90.2 43.3 75 A LEU CG 323 205.1 90.0 44.7 73 A LEU CD1 323 206.6 89.6 44.7 72 A LEU CD2 323 204.8 91.2 45.5 73 A LEU C 323 204.2 89.0 41.1 78 A LEU O 323 203.8 87.9 41.0 79 A GLU N 324 203.8 89.9 40.2 82 A GLU CA 324 202.9 89.7 39.1 85 A GLU CB 324 202.7 90.8 38.2 86 A GLU CG 324 202.1 92.1 38.7 87 A GLU CD 324 202.1 93.3 37.6 88 A GLU OE1 324 201.6 93.1 36.6 88 A GLU OE2 324 202.7 94.3 37.9 88 A GLU C 324 203.4 88.5 38.3 86 A GLU O 324 202.7 87.6 37.9 87 A ASN N 325 204.7 88.5 38.1 88 A ASN CA 325 205.4 87.5 37.4 91 A ASN CB 325 206.6 88.1 36.6 90 A ASN CG 325 206.1 89.0 35.4 90 A ASN OD1 325 207.0 89.6 34.7 90 A ASN ND2 325 204.8 89.1 35.3 89 A ASN C 325 205.9 86.3 38.2 93 A ASN O 325 206.5 85.3 37.6 94 A GLN N 326 205.7 86.3 39.5 95 A GLN CA 326 206.1 85.2 40.4 98 A GLN CB 326 205.4 83.9 40.0 98 A GLN CG 326 204.1 83.7 40.7 98 A GLN CD 326 203.2 84.9 40.7 98 A GLN OE1 326 202.8 85.5 39.7 97 A GLN NE2 326 202.8 85.4 41.9 98 A GLN C 326 207.6 85.0 40.5 99 A GLN O 326 208.3 84.8 39.4 0 CYS N 327 208.2 85.1 41.7 0 CYS CA 327 209.6 85.0 41.8 0 CYS CB 327 210.3 86.3 41.7 0 CYS SG 327 212.1 86.2 41.7 0 CYS C 327 210.0 84.3 43.1 0 CYS O 327 209.2 84.5 44.1 0 ASP N 328 211.1 83.5 43.2 0 ASP CA 328 211.5 82.9 44.4 0 ASP CB 328 212.7 82.0 44.2 0 ASP CG 328 212.8 80.8 45.2 0 ASP OD1 328 212.2 80.8 46.3 0 ASP OD2 328 213.6 79.8 44.9 0 ASP C 328 211.8 84.0 45.4 0 ASP O 328 212.2 85.1 45.0 0 ASN N 329 211.6 83.7 46.7 0 ASN CA 329 211.8 84.6 47.8 0 ASN CB 329 213.1 85.4 47.6 0 ASN CG 329 214.3 84.5 47.4 0 ASN OD1 329 214.8 83.9 48.4 0 ASN ND2 329 214.7 84.3 46.2 0 ASN C 329 210.6 85.6 47.8 0 ASN O 329 210.6 86.5 48.5 0 LYS N 330 209.6 85.3 46.9 0 LYS CA 330 208.4 86.2 46.8 0 LYS CB 330 207.3 85.6 45.9 0 LYS CG 330 206.5 84.5 46.5 0 LYS CD 330 205.0 84.7 46.3 0 LYS CE 330 204.7 85.1 44.9 0 LYS NZ 330 205.0 84.1 43.8 0 LYS C 330 207.8 86.6 48.2 0 LYS O 330 207.3 87.7 48.3 0 GLU N 331 207.9 85.7 49.1 0 GLU CA 331 207.4 86.0 50.4 0 GLU CB 331 207.4 84.8 51.4 0 GLU CG 331 206.6 85.0 52.7 0 GLU CD 331 205.3 85.8 52.4 0 GLU OE1 331 204.5 85.3 51.7 0 GLU OE2 331 205.2 86.9 53.1 0 GLU C 331 208.1 87.2 51.1 0 GLU O 331 207.5 88.1 51.6 0 ASP N 332 209.5 87.1 51.0 99 A ASP CA 332 210.3 88.2 51.6 97 A ASP CB 332 211.8 87.8 51.5 99 A ASP CG 332 212.7 88.8 52.2 0 ASP OD1 332 213.7 89.2 51.5 0 ASP OD2 332 212.5 89.2 53.3 0 ASP C 332 210.1 89.4 50.7 95 A ASP O 332 209.9 90.5 51.3 95 A ILE N 333 210.1 89.3 49.4 91 A ILE CA 333 209.8 90.4 48.5 87 A ILE CB 333 209.7 89.9 47.0 87 A ILE CG2 333 209.1 90.9 46.2 87 A ILE CG1 333 211.1 89.6 46.5 87 A ILE CD1 333 211.2 89.0 45.1 87 A ILE C 333 208.6 91.1 48.9 85 A ILE O 333 208.6 92.3 49.1 84 A LEU N 334 207.5 90.4 49.2 83 A LEU CA 334 206.3 91.0 49.6 82 A LEU CB 334 205.2 89.9 49.7 81 A LEU CG 334 203.8 90.4 50.2 81 A LEU CD1 334 203.3 91.5 49.3 80 A LEU CD2 334 202.8 89.2 50.2 81 A LEU C 334 206.4 91.7 51.0 82 A LEU O 334 205.7 92.7 51.2 83 A ASN N 335 207.3 91.1 51.8 82 A ASN CA 335 207.5 91.7 53.2 81 A ASN CB 335 208.2 90.7 54.1 81 A ASN CG 335 207.5 89.4 54.3 81 A ASN OD1 335 206.2 89.4 54.4 81 A ASN ND2 335 208.2 88.4 54.5 81 A ASN C 335 208.2 93.0 53.0 80 A ASN O 335 207.8 94.0 53.6 79 A LYS N 336 209.3 93.0 52.2 78 A LYS CA 336 210.1 94.2 52.0 77 A LYS CB 336 211.2 93.9 51.0 78 A LYS CG 336 212.1 95.1 50.6 79 A LYS CD 336 212.5 95.9 51.7 80 A LYS CE 336 213.3 97.2 51.2 81 A LYS NZ 336 213.6 98.1 52.4 81 A LYS C 336 209.2 95.3 51.4 75 A LYS O 336 209.2 96.5 51.8 74 A ALA N 337 208.4 94.9 50.4 72 A ALA CA 337 207.5 95.9 49.7 70 A ALA CB 337 206.9 95.2 48.5 69 A ALA C 337 206.4 96.5 50.6 68 A ALA O 337 206.0 97.6 50.4 69 A LEU N 338 205.9 95.7 51.5 66 A LEU CA 338 204.8 96.2 52.4 64 A LEU CB 338 204.1 95.0 53.0 64 A LEU CG 338 203.3 94.1 52.0 63 A LEU CD1 338 203.0 92.8 52.7 63 A LEU CD2 338 202.0 94.9 51.6 63 A LEU C 338 205.4 97.1 53.5 63 A LEU O 338 204.7 98.0 54.0 61 A GLU N 339 206.6 96.9 53.8 62 A GLU CA 339 207.4 97.6 54.8 62 A GLU CB 339 208.7 96.9 55.2 64 A GLU CG 339 209.6 97.7 56.0 67 A GLU CD 339 211.0 97.7 55.5 69 A GLU OE1 339 211.8 98.5 55.8 70 A GLU OE2 339 211.3 96.8 54.6 70 A GLU C 339 207.6 99.0 54.2 59 A GLU O 339 207.5 100.0 54.9 58 A LEU N 340 208.0 99.0 52.9 56 A LEU CA 340 208.3 100.2 52.2 54 A LEU CB 340 208.8 99.9 50.8 51 A LEU CG 340 210.2 99.2 50.7 50 A LEU CD1 340 210.5 99.1 49.2 49 A LEU CD2 340 211.2 100.1 51.4 49 A LEU C 340 206.9 101.0 52.1 55 A LEU O 340 206.9 102.2 52.2 56 A CYS N 341 205.8 100.2 51.9 54 A CYS CA 341 204.5 100.9 51.8 55 A CYS CB 341 203.4 99.9 51.4 55 A CYS SG 341 203.3 99.5 49.7 54 A CYS C 341 204.1 101.5 53.1 56 A CYS O 341 203.4 102.6 53.1 55 A GLU N 342 204.6 101.0 54.3 58 A GLU CA 342 204.3 101.6 55.6 59 A GLU CB 342 204.4 100.5 56.7 61 A GLU CG 342 203.0 99.9 57.0 65 A GLU CD 342 201.9 100.8 56.8 67 A GLU OE1 342 201.6 101.7 57.7 68 A GLU OE2 342 201.2 100.8 55.7 68 A GLU C 342 205.2 102.7 55.9 59 A GLU O 342 204.8 103.7 56.6 59 A ILE N 343 206.5 102.7 55.5 59 A ILE CA 343 207.4 103.8 55.6 58 A ILE CB 343 208.8 103.4 55.1 57 A ILE CG2 343 209.7 104.6 55.2 57 A ILE CG1 343 209.3 102.2 55.8 58 A ILE CD1 343 210.5 101.5 55.2 60 A ILE C 343 206.9 105.0 54.9 58 A ILE O 343 206.8 106.1 55.4 58 A LEU N 344 206.6 104.8 53.6 57 A LEU CA 344 206.0 105.8 52.8 57 A LEU CB 344 205.8 105.3 51.3 56 A LEU CG 344 207.0 105.0 50.5 55 A LEU CD1 344 206.7 104.3 49.2 55 A LEU CD2 344 207.7 106.3 50.2 55 A LEU C 344 204.7 106.3 53.4 57 A LEU O 344 204.5 107.5 53.5 57 A ALA N 345 203.8 105.4 53.8 58 A ALA CA 345 202.5 105.8 54.4 59 A ALA CB 345 201.6 104.6 54.4 58 A ALA C 345 202.6 106.5 55.8 60 A ALA O 345 201.8 107.4 56.0 59 A LYS N 346 203.5 106.0 56.6 62 A LYS CA 346 203.7 106.5 58.0 63 A LYS CB 346 204.0 105.4 58.9 66 A LYS CG 346 202.9 104.4 59.2 68 A LYS CD 346 203.5 103.2 60.0 70 A LYS CE 346 202.4 102.1 60.4 71 A LYS NZ 346 203.0 100.8 60.8 71 A LYS C 346 204.7 107.6 58.1 63 A LYS O 346 204.6 108.5 58.9 64 A GLU N 347 205.9 107.4 57.4 63 A GLU CA 347 207.0 108.4 57.5 63 A GLU CB 347 208.2 107.6 58.1 65 A GLU CG 347 209.5 108.4 58.0 69 A GLU CD 347 210.7 107.7 58.7 72 A GLU OE1 347 210.7 107.6 60.0 74 A GLU OE2 347 211.6 107.2 58.0 73 A GLU C 347 207.4 109.1 56.3 61 A GLU O 347 207.4 110.3 56.2 60 A LYS N 348 207.9 108.4 55.3 59 A LYS CA 348 208.4 108.9 54.1 58 A LYS CB 348 209.1 107.8 53.3 60 A LYS CG 348 210.5 108.1 52.8 62 A LYS CD 348 211.6 107.7 53.9 64 A LYS CE 348 211.6 108.7 55.1 64 A LYS NZ 348 212.8 108.4 56.0 65 A LYS C 348 207.6 109.7 53.1 56 A LYS O 348 208.1 110.6 52.4 57 A ASP N 349 206.3 109.5 53.1 54 A ASP CA 349 205.4 110.3 52.1 51 A ASP CB 349 205.6 109.8 50.7 51 A ASP CG 349 204.8 110.6 49.7 51 A ASP OD1 349 204.9 111.8 49.7 51 A ASP OD2 349 204.1 109.9 48.9 51 A ASP C 349 203.9 110.2 52.5 50 A ASP O 349 203.1 109.7 51.8 50 A THR N 350 203.6 110.8 53.7 49 A THR CA 350 202.3 110.7 54.3 47 A THR CB 350 202.3 111.1 55.7 48 A THR OG1 350 202.2 112.5 55.9 50 A THR CG2 350 203.6 110.6 56.4 49 A THR C 350 201.2 111.5 53.6 46 A THR O 350 200.0 111.4 54.0 46 A ILE N 351 201.5 112.4 52.7 46 A ILE CA 351 200.4 113.2 52.1 44 A ILE CB 351 200.9 114.3 51.1 43 A ILE CG2 351 201.4 113.7 49.8 41 A ILE CG1 351 199.8 115.3 50.9 43 A ILE CD1 351 199.3 116.0 52.1 42 A ILE C 351 199.4 112.2 51.4 45 A ILE O 351 198.2 112.4 51.4 45 A ARG N 352 200.0 111.1 50.9 46 A ARG CA 352 199.2 110.1 50.2 48 A ARG CB 352 199.7 109.8 48.8 48 A ARG CG 352 201.1 109.9 48.5 47 A ARG CD 352 201.4 110.5 47.1 47 A ARG NE 352 202.6 111.4 47.1 48 A ARG CZ 352 202.6 112.7 46.9 48 A ARG NH1 352 201.5 113.4 46.7 48 A ARG NH2 352 203.7 113.4 47.1 48 A ARG C 352 199.3 108.8 51.0 51 A ARG O 352 199.9 107.8 50.6 52 A LYS N 353 198.8 108.8 52.3 53 A LYS CA 353 198.8 107.7 53.2 53 A LYS CB 353 198.7 108.2 54.6 53 A LYS CG 353 197.5 108.9 55.0 55 A LYS CD 353 197.5 109.7 56.3 55 A LYS CE 353 196.2 110.4 56.6 55 A LYS NZ 353 196.3 111.4 57.7 55 A LYS C 353 197.7 106.8 52.8 53 A LYS O 353 197.7 105.6 53.1 53 A GLU N 354 196.6 107.4 52.2 53 A GLU CA 354 195.4 106.7 51.8 53 A GLU CB 354 194.4 107.7 51.3 56 A GLU CG 354 193.7 108.4 52.4 59 A GLU CD 354 193.1 107.4 53.5 61 A GLU OE1 354 193.6 107.3 54.6 63 A GLU OE2 354 192.1 106.7 53.1 63 A GLU C 354 195.8 105.8 50.6 53 A GLU O 354 195.3 104.7 50.5 54 A TYR N 355 196.7 106.3 49.7 50 A TYR CA 355 197.1 105.6 48.6 49 A TYR CB 355 197.7 106.5 47.5 45 A TYR CG 355 198.4 105.8 46.4 41 A TYR CD1 355 197.7 105.3 45.3 39 A TYR CE1 355 198.3 104.7 44.3 38 A TYR CD2 355 199.8 105.6 46.4 39 A TYR CE2 355 200.4 105.0 45.4 38 A TYR CZ 355 199.7 104.5 44.3 38 A TYR OH 355 200.3 103.9 43.3 41 A TYR C 355 198.1 104.5 48.9 51 A TYR O 355 197.9 103.3 48.5 52 A TRP N 356 199.1 104.9 49.7 53 A TRP CA 356 200.2 104.0 50.1 55 A TRP CB 356 201.2 104.7 50.9 55 A TRP CG 356 202.1 105.4 49.9 55 A TRP CD2 3S6 202.7 104.8 48.8 54 A TRP CE2 356 203.5 105.8 48.2 55 A TRP CE3 356 202.7 103.6 48.2 55 A TRP CD1 356 202.6 106.7 50.0 54 A TRP NE1 356 203.4 107.0 48.9 55 A TRP CZ2 356 204.3 105.6 47.0 55 A TRP CZ3 356 203.4 103.3 47.0 55 A TRP CH2 356 204.2 104.3 46.5 55 A TRP C 356 199.7 102.7 51.0 56 A TRP O 356 200.4 101.7 51.0 56 A ARG N 357 198.7 102.9 51.8 58 A ARG CA 357 198.2 101.8 52.6 60 A ARG CB 357 197.4 102.3 53.8 60 A ARG CG 357 198.3 102.9 54.9 62 A ARG CD 357 197.6 103.1 56.2 64 A ARG NE 357 196.4 103.8 56.1 65 A ARG CZ 357 196.3 105.1 56.4 65 A ARG NH1 357 195.1 105.7 56.2 65 A ARG NH2 357 197.3 105.8 56.8 66 A ARG C 357 197.3 101.0 51.7 59 A ARG O 357 197.2 99.8 51.8 61 A TYR N 358 196.7 101.6 50.7 57 A TYR CA 358 195.8 100.9 49.7 55 A TYR CB 358 195.0 101.9 48.9 55 A TYR CG 358 194.6 101.3 47.6 54 A TYR CD1 358 193.3 100.7 47.5 54 A TYR CE1 358 192.9 100.1 46.3 54 A TYR CD2 358 195.4 101.2 46.5 54 A TYR CE2 358 195.0 100.6 45.3 54 A TYR CZ 358 193.8 100.0 45.2 54 A TYR OH 358 193.4 99.4 44.0 52 A TYR C 358 196.7 100.0 48.9 55 A TYR O 358 196.2 99.0 48.4 55 A ILE N 359 197.9 100.5 48.6 56 A ILE CA 359 198.8 99.6 47.8 57 A ILE CB 359 200.0 100.5 47.3 57 A ILE CG2 359 201.1 99.6 46.5 55 A ILE CG1 359 199.5 101.5 46.3 56 A ILE CD1 359 198.8 101.0 45.1 56 A ILE C 359 199.4 98.5 48.7 59 A ILE O 359 199.9 97.5 48.2 59 A GLY N 360 199.2 98.7 50.0 60 A GLY CA 360 199.6 97.6 50.9 60 A GLY C 360 198.6 96.5 50.9 60 A GLY O 360 198.9 95.4 50.9 60 A ARG N 361 197.3 97.0 50.9 61 A ARG CA 361 196.2 96.1 50.9 62 A ARG CB 361 194.9 96.8 51.3 62 A ARG CG 361 194.9 97.4 52.7 63 A ARG CD 361 193.6 97.9 53.2 64 A ARG NE 361 193.0 98.9 52.3 67 A ARG CZ 361 193.4 100.2 52.4 68 A ARG NH1 361 192.8 101.1 51.6 69 A ARG NH2 361 194.4 100.6 53.2 69 A ARG C 361 196.0 95.3 49.6 63 A ARG O 361 195.5 94.2 49.6 65 A SER N 362 196.3 96.0 48.5 63 A SER CA 362 196.1 95.3 47.2 64 A SER CB 362 196.1 96.3 46.1 63 A SER OG 362 194.9 97.1 46.1 64 A SER C 362 197.2 94.3 47.0 65 A SER O 362 197.1 93.3 46.5 65 A LEU N 363 198.4 94.7 47.6 66 A LEU CA 363 199.6 93.8 47.6 67 A LEU CB 363 200.8 94.6 48.1 66 A LEU CG 363 202.1 94.6 47.3 66 A LEU CD1 363 201.8 94.6 45.8 65 A LEU CD2 363 202.9 95.9 47.7 65 A LEU C 363 199.3 92.5 48.4 69 A LEU O 363 200.1 91.6 48.4 68 A GLN N 364 198.2 92.5 49.2 72 A GLN CA 364 197.8 91.4 50.0 75 A GLN CB 364 196.9 91.8 51.1 76 A GLN CG 364 197.6 92.7 52.1 77 A GLN CD 364 199.0 92.2 52.5 78 A GLN OE1 364 199.2 91.6 53.5 79 A GLN NE2 364 200.0 92.5 51.6 78 A GLN C 364 197.1 90.4 49.1 78 A GLN O 364 197.5 89.3 48.9 79 A SER N 365 196.0 90.9 48.5 80 A SER CA 365 195.2 90.1 47.6 83 A SER CB 365 194.0 90.9 47.1 83 A SER OG 365 193.2 91.4 48.2 83 A SER C 365 196.0 89.7 46.4 86 A SER O 365 196.2 88.5 46.2 86 A LYS N 366 196.6 90.6 45.7 89 A LYS CA 366 197.4 90.3 44.5 92 A LYS CB 366 196.6 90.7 43.2 93 A LYS CG 366 195.9 92.1 43.2 94 A LYS CD 366 194.6 92.2 44.0 94 A LYS CE 366 194.1 93.6 44.2 94 A LYS NZ 366 192.9 93.6 45.1 94 A LYS C 366 198.8 90.9 44.4 93 A LYS OT1 366 199.8 90.1 44.5 93 A LYS OT2 366 199.0 92.2 44.3 93 A LEU CB 523 196.2 122.2 61.7 47 B LEU CG 523 194.9 123.0 62.1 48 B LEU CD1 523 195.1 124.4 61.7 48 B LEU CD2 523 193.7 122.4 61.4 48 B LEU C 523 197.5 120.0 61.6 48 B LEU O 523 198.6 120.2 62.0 49 B LEU N 523 196.5 120.8 63.7 49 B LEU CA 523 196.3 120.7 62.2 48 B TYR N 524 197.2 119.1 60.6 47 B TYR CA 524 198.2 118.4 59.9 47 B TYR CB 524 197.5 117.6 58.8 46 B TYR CG 524 198.5 116.9 57.9 46 B TYR CD1 524 199.3 115.8 58.4 47 B TYR CE1 524 200.2 115.1 57.7 47 B TYR CD2 524 198.7 117.2 56.6 47 B TYR CE2 524 199.6 116.5 55.8 47 B TYR CZ 524 200.4 115.4 56.3 47 B TYR OH 524 201.2 114.8 55.5 47 B TYR C 524 199.3 119.3 59.5 47 B TYR O 524 200.5 119.0 59.7 45 B SER N 525 198.9 120.5 58.9 48 B SER CA 525 199.8 121.5 58.4 49 B SER CB 525 199.0 122.5 57.6 48 B SER OG 525 198.3 121.9 56.5 49 B SER C 525 200.7 122.2 59.4 51 B SER O 525 201.9 122.5 59.1 51 B LEU N 526 200.1 122.7 60.5 52 B LEU CA 526 200.8 123.5 61.5 52 B LEU CB 526 199.8 124.3 62.3 52 B LEU CG 526 198.7 125.1 61.7 52 B LEU CD1 526 198.0 126.0 62.7 52 B LEU CD2 526 199.2 126.0 60.5 51 B LEU C 526 201.7 122.6 62.4 53 B LEU O 526 202.4 123.1 63.3 53 B ARG N 527 201.7 121.3 62.1 53 B ARG CA 527 202.5 120.4 62.9 55 B ARG CB 527 202.2 118.9 62.7 54 B ARG CG 527 200.8 118.5 63.2 54 B ARG CD 527 200.4 117.1 62.9 53 B ARG NE 527 199.0 117.0 63.1 54 B ARG CZ 527 198.3 116.0 62.5 54 B ARG NH1 527 198.9 115.1 61.7 55 B ARG NH2 527 197.0 116.0 62.6 54 B ARG C 527 204.0 120.6 62.6 57 B ARG O 527 204.3 121.3 61.6 58 B PRO N 528 204.9 120.2 63.5 59 B PRO CD 528 204.5 120.0 65.0 60 B PRO CA 528 206.3 120.4 63.4 61 B PRO CB 528 206.8 120.2 64.9 60 B PRO CG 528 205.7 120.7 65.7 60 B PRO C 528 207.1 119.4 62.5 62 B PRO O 528 208.1 119.8 62.0 63 B GLU N 529 206.5 118.2 62.3 63 B GLU CA 529 207.2 117.3 61.4 64 B GLU CB 529 206.8 115.8 61.8 66 B GLU CG 529 205.3 115.5 62.1 68 B GLU CD 529 204.9 115.7 63.5 69 B GLU OE1 529 203.7 116.1 63.8 69 B GLU OE2 529 205.7 115.5 64.4 70 B GLU C 529 206.8 117.6 59.9 64 B GLU O 529 207.6 117.2 59.0 65 B HIS N 530 205.7 118.2 59.7 64 B HIS CA 530 205.2 118.6 58.4 64 B HIS CB 530 203.9 119.3 58.5 64 B HIS CG 530 203.4 120.0 57.2 63 B HIS CD2 530 202.7 119.6 56.2 62 B HIS ND1 530 203.8 121.3 56.9 63 B HIS CE1 530 203.2 121.7 55.7 62 B HIS NE2 530 202.6 120.6 55.3 62 B HIS C 530 206.2 119.6 57.7 63 B HIS O 530 206.3 119.7 56.5 64 B ALA N 531 207.0 120.2 58.5 63 B ALA CA 531 208.0 121.1 58.0 63 B ALA CB 531 208.6 121.9 59.1 64 B ALA C 531 209.2 120.4 57.3 63 B ALA O 531 210.0 121.0 56.6 63 B ARG N 532 209.2 119.1 57.4 63 B ARG CA 532 210.2 118.3 56.7 64 B ARG CB 532 210.3 116.9 57.5 69 B ARG CG 532 210.8 117.1 58.9 74 B ARG CD 532 210.5 115.9 59.8 79 B ARG NE 532 211.3 116.0 61.0 84 B ARG CZ 532 211.6 114.9 61.7 86 B ARG NH1 532 212.4 115.1 62.8 88 B ARG NH2 532 211.3 113.7 61.3 87 B ARG C 532 209.7 118.0 55.3 62 B ARG O 532 210.4 117.4 54.5 62 B GLU N 533 208.4 118.4 55.1 58 B GLU CA 533 207.8 118.2 53.7 57 B GLU CB 533 206.3 118.1 53.8 56 B GLU CG 533 205.9 116.8 54.6 56 B GLU CD 533 206.2 115.5 53.9 56 B GLU OE1 533 205.2 114.8 53.6 57 B GLU OE2 533 207.3 115.2 53.7 56 B GLU C 533 208.3 119.3 52.8 55 B GLU O 533 207.8 119.3 51.7 56 B ARG N 534 209.2 120.1 53.3 53 B ARG CA 534 209.7 121.3 52.5 50 B ARG CB 534 210.6 122.1 53.4 51 B ARG CG 534 210.7 123.5 53.1 52 B ARG CD 534 209.4 124.3 53.4 52 B ARG NE 534 209.5 125.6 52.8 54 B ARG CZ 534 209.6 126.8 53.4 54 B ARG NH1 534 209.5 126.8 54.8 55 B ARG NH2 534 209.7 127.9 52.8 54 B ARG C 534 210.5 120.7 51.3 48 B ARG O 534 210.9 119.6 51.3 46 B LEU N 535 210.7 121.6 50.3 46 B LEU CA 535 211.4 121.2 49.0 44 B LEU CB 535 211.2 122.3 48.0 40 B LEU CG 535 212.0 122.2 46.7 38 B LEU CD1 535 211.7 121.0 45.9 36 B LEU CD2 535 211.9 123.4 45.8 37 B LEU C 535 212.8 120.9 49.2 45 B LEU O 535 213.6 121.6 49.7 45 B GLN N 536 213.2 119.7 48.6 47 B GLN CA 536 214.6 119.2 48.6 50 B GLN CB 536 214.6 117.7 48.6 52 B GLN CG 536 213.7 117.1 49.6 54 B GLN CD 536 214.2 117.0 51.0 56 B GLN OE1 536 215.3 116.4 51.2 56 B GLN NE2 536 213.6 117.7 51.9 56 B GLN C 536 215.1 119.7 47.2 51 B GLN O 536 214.7 119.0 46.2 51 B ASP N 537 215.8 120.8 47.2 52 B ASP CA 537 216.3 121.4 46.0 53 B ASP CB 537 216.8 122.8 46.3 55 B ASP CG 537 217.7 123.4 45.2 58 B ASP OD1 537 218.7 124.1 45.6 60 B ASP OD2 537 217.4 123.2 44.1 60 B ASP C 537 217.4 120.6 45.3 52 B ASP O 537 217.7 120.7 44.1 50 B ASP N 538 218.1 119.7 46.0 52 B ASP CA 538 219.3 118.9 45.5 52 B ASP CB 538 218.9 118.1 44.3 53 B ASP CG 538 217.8 117.0 44.5 54 B ASP OD1 538 217.9 116.3 45.6 54 B ASP OD2 538 216.9 116.9 43.7 55 B ASP C 538 220.5 119.8 45.2 51 B ASP O 538 221.5 119.3 44.7 49 B SER N 539 220.4 121.0 45.6 51 B SER CA 539 221.4 122.1 45.4 52 B SER CB 539 222.7 121.6 45.9 53 B SER OG 539 222.7 121.3 47.3 55 B SER C 539 221.5 122.4 43.9 52 B SER O 539 222.3 123.2 43.5 54 B VAL N 540 220.6 121.7 43.1 50 B VAL CA 540 220.6 121.9 41.7 48 B VAL CB 540 220.5 120.6 41.0 47 B VAL CG1 540 220.6 120.8 39.5 46 B VAL CG2 540 221.7 119.7 41.4 46 B VAL C 540 219.3 122.7 41.5 47 B VAL O 540 218.3 122.2 41.2 49 B GLU N 541 219.4 124.0 41.6 47 B GLU CA 541 218.3 124.9 41.5 47 B GLU CB 541 218.4 126.1 42.4 49 B GLU CG 541 219.7 126.9 42.1 53 B GLU CD 541 220.0 127.9 43.2 55 B GLU OE1 541 221.0 127.7 44.0 57 B GLU OE2 541 219.2 128.9 43.3 55 B GLU C 541 218.0 125.3 40.1 45 B GLU O 541 218.9 125.8 39.3 46 B THR N 542 216.7 125.2 39.7 41 B THR CA 542 216.3 125.5 38.3 38 B THR CB 542 215.8 124.4 37.5 38 B THR OG1 542 214.6 123.8 38.1 38 B THR CG2 542 216.9 123.3 37.4 37 B THR C 542 215.1 126.5 38.5 37 B THR O 542 214.6 126.6 39.6 37 B VAL N 543 214.7 127.0 37.4 35 B VAL CA 543 213.5 127.9 37.4 34 B VAL CB 543 213.1 128.3 36.0 35 B VAL CG1 543 212.0 129.3 36.0 34 B VAL CG2 543 214.2 128.8 35.2 35 B VAL C 543 212.3 127.3 38.1 34 B VAL O 543 211.5 128.0 38.7 35 B THR N 544 212.3 126.0 38.1 34 B THR CA 544 211.2 125.3 38.8 34 B THR CB 544 211.0 123.9 38.3 35 B THR OG1 544 211.0 123.8 36.9 35 B THR CG2 544 209.6 123.3 38.8 34 B THR C 544 211.3 125.3 40.4 34 B THR O 544 210.3 125.5 41.1 35 B SER N 545 212.5 125.0 40.8 34 B SER CA 545 212.8 124.9 42.3 33 B SER CB 545 214.3 124.6 42.5 33 B SER OG 545 214.9 123.8 41.5 35 B SER C 545 212.5 126.2 42.9 33 B SER O 545 211.8 126.3 43.8 34 B ILE N 546 213.1 127.3 42.3 33 B ILE CA 546 213.0 128.6 42.7 32 B ILE CB 546 213.6 129.6 41.6 31 B ILE CG2 546 213.3 131.0 41.9 30 B ILE CG1 546 215.1 129.3 41.5 31 B ILE CD1 546 215.7 130.0 40.3 32 B ILE C 546 211.5 129.0 42.9 34 B ILE O 546 211.2 129.5 44.0 35 B GLU N 547 210.7 128.8 41.9 33 B GLU CA 547 209.3 129.2 42.0 34 B GLU CB 547 208.6 129.0 40.6 35 B GLU CG 547 209.1 130.0 39.6 35 B GLU CD 547 209.1 131.4 40.1 37 B GLU OE1 547 208.1 132.0 40.5 38 B GLU OE2 547 210.2 132.0 40.1 39 B GLU C 547 208.6 128.4 43.0 32 B GLU O 547 207.8 129.0 43.8 33 B GLN N 548 208.8 127.1 43.1 32 B GLN CA 548 208.2 126.2 44.1 31 B GLN CB 548 208.6 124.8 43.9 29 B GLN CG 548 208.0 123.8 44.9 26 B GLN CD 548 206.5 123.8 44.9 25 B GLN OE1 548 205.9 123.5 45.9 26 B GLN NE2 548 205.9 124.2 43.8 25 B GLN C 548 208.5 126.7 45.5 33 B GLN O 548 207.7 127.0 46.3 34 B ALA N 549 209.8 126.9 45.7 34 B ALA CA 549 210.3 127.4 47.0 35 B ALA CB 549 211.8 127.5 46.9 35 B ALA C 549 209.7 128.8 47.3 36 B ALA O 549 209.5 129.0 48.5 39 B LYS N 550 209.3 129.6 46.3 36 B LYS CA 550 208.7 130.8 46.6 38 B LYS CB 550 208.6 131.7 45.4 38 B LYS CG 550 209.9 132.2 44.9 40 B LYS CD 550 209.7 133.1 43.7 42 B LYS CE 550 211.0 133.5 43.0 43 B LYS NZ 550 210.7 134.2 41.8 46 B LYS C 550 207.3 130.6 47.2 39 B LYS O 550 206.9 131.3 48.2 40 B VAL N 551 206.6 129.8 46.6 40 B VAL CA 551 205.2 129.5 47.0 41 B VAL CB 551 204.4 128.6 46.1 40 B VAL CG1 551 203.0 128.4 46.6 40 B VAL CG2 551 204.4 129.2 44.7 40 B VAL C 551 205.3 128.9 48.4 42 B VAL O 551 204.6 129.4 49.3 42 B GLU N 552 206.2 128.0 48.7 42 B GLU CA 552 206.3 127.4 50.0 43 B GLU CB 552 207.4 126.3 49.9 42 B GLU CG 552 207.0 125.1 49.2 40 B GLU CD 552 208.0 124.0 49.2 40 B GLU OE1 552 209.1 124.1 49.7 41 B GLU OE2 552 207.7 122.9 48.6 40 B GLU C 552 206.6 128.3 51.1 45 B GLU O 552 206.0 128.2 52.2 45 B GLU N 553 207.4 129.4 50.8 48 B GLU CA 553 207.6 130.4 51.8 50 B GLU CB 553 208.8 131.3 51.5 54 B GLU CG 553 210.2 130.9 52.1 59 B GLU CD 553 210.2 130.9 53.7 63 B GLU OE1 553 210.9 130.0 54.3 64 B GLU OE2 553 209.5 131.7 54.3 65 B GLU C 553 206.4 131.2 52.1 49 B GLU O 553 206.0 131.5 53.3 49 B LYS N 554 205.6 131.7 51.1 49 B LYS CA 554 204.4 132.5 51.3 49 B LYS CB 554 203.9 132.9 49.9 51 B LYS CG 554 204.9 133.5 49.0 55 B LYS CD 554 204.3 133.9 47.6 58 B LYS CE 554 203.9 132.7 46.7 58 B LYS NZ 554 203.4 133.2 45.3 58 B LYS C 554 203.4 131.6 52.0 49 B LYS O 554 202.5 132.2 52.7 48 B ILE N 555 203.4 130.3 51.8 49 B ILE CA 555 202.5 129.4 52.4 49 B ILE CB 555 202.4 128.1 51.7 49 B ILE CG2 555 201.4 127.1 52.4 49 B ILE CG1 555 201.9 128.2 50.2 49 B ILE CD1 555 200.5 128.9 50.1 48 B ILE C 555 202.9 129.2 53.9 49 B ILE O 555 202.1 129.2 54.8 50 B GLN N 556 204.2 129.0 54.1 50 B GLN CA 556 204.7 128.8 55.4 51 B GLN CB 556 206.2 128.7 55.4 51 B GLN CG 556 206.8 128.3 56.8 53 B GLN CD 556 206.3 127.0 57.4 54 B GLN OE1 556 206.8 125.9 57.2 54 B GLN NE2 556 205.2 127.1 58.1 54 B GLN C 556 204.2 129.9 56.3 53 B GLN O 556 203.5 129.6 57.3 53 B GLU N 557 204.4 131.1 55.8 54 B GLU CA 557 203.9 132.3 56.6 54 B GLU CB 557 203.9 133.6 55.7 58 B GLU CG 557 205.3 134.1 55.4 62 B GLU CD 557 205.3 135.3 54.5 65 B GLU OE1 557 204.3 136.0 54.4 66 B GLU OE2 557 206.4 135.6 53.8 66 B GLU C 557 202.5 132.1 57.0 53 B GLU O 557 202.2 132.2 58.2 55 B VAL N 558 201.6 131.8 56.1 50 B VAL CA 558 200.2 131.6 56.4 49 B VAL CB 558 199.4 131.1 55.2 49 B VAL CG1 558 198.0 130.7 55.6 48 B VAL CG2 558 199.3 132.2 54.1 48 B VAL C 558 200.0 130.5 57.5 48 B VAL O 558 199.3 130.7 58.4 49 B PHE N 559 200.8 129.5 57.3 48 B PHE CA 559 200.7 128.4 58.3 47 B PHE CB 559 201.6 127.2 57.9 44 B PHE CG 559 201.0 126.4 56.8 42 B PHE CD1 559 201.7 125.4 56.1 42 B PHE CD2 559 199.6 126.5 56.4 42 B PHE CE1 559 201.2 124.6 55.1 41 B PHE CE2 559 199.1 125.8 55.4 41 B PHE CZ 559 199.8 124.8 54.8 41 B PHE C 559 201.1 129.0 59.7 48 B PHE O 559 200.3 129.0 60.6 48 B SER N 560 202.3 129.5 59.8 50 B SER CA 560 202.8 130.1 61.0 52 B SER CB 560 204.2 130.5 60.9 52 B SER OG 560 205.0 129.3 60.6 54 B SER C 560 202.0 131.3 61.4 55 B SER O 560 202.3 131.9 62.5 55 B SER N 561 201.0 131.7 60.6 58 B SER CA 561 200.2 132.9 61.0 62 B SER CB 561 199.0 132.9 60.1 64 B SER OG 561 198.1 134.0 60.5 66 B SER C 561 199.8 133.0 62.4 65 B SER O 561 199.9 134.0 63.1 66 B TYR N 562 199.4 131.8 63.0 69 B TYR CA 562 198.9 131.6 64.3 71 B TYR CB 562 198.3 130.2 64.4 72 B TYR CG 562 197.3 130.0 63.3 74 B TYR CD1 562 197.7 129.4 62.1 74 B TYR CE1 562 196.9 129.3 61.0 75 B TYR CD2 562 196.1 130.6 63.3 75 B TYR CE2 562 195.2 130.5 62.2 75 B TYR CZ 562 195.6 129.9 61.1 75 B TYR OH 562 194.8 129.9 60.0 76 B TYR C 562 200.0 131.8 65.4 72 B TYR O 562 199.8 132.6 66.3 71 B LYS N 563 201.1 131.1 65.3 73 B LYS CA 563 202.2 131.1 66.2 74 B LYS CB 563 203.4 130.3 65.6 76 B LYS CG 563 203.0 128.9 65.2 79 B LYS CD 563 204.2 128.1 64.7 80 B LYS CE 563 203.8 126.6 64.3 81 B LYS NZ 563 204.9 125.8 63.8 82 B LYS C 563 202.6 132.5 66.5 74 B LYS O 563 202.6 133.0 67.6 73 B PHE N 564 202.9 133.3 65.4 75 B PHE CA 564 203.4 134.7 65.6 77 B PHE CB 564 203.6 135.3 64.2 80 B PHE CG 564 204.8 134.8 63.5 83 B PHE CD1 564 205.1 133.5 63.2 85 B PHE CD2 564 205.8 135.8 63.0 85 B PHE CE1 564 206.2 133.1 62.5 85 B PHE CE2 564 206.9 135.4 62.3 86 B PHE CZ 564 207.1 134.0 62.0 86 B PHE C 564 202.4 135.6 66.3 76 B PHE O 564 202.8 136.4 67.1 75 B ASN N 565 201.1 135.4 66.1 75 B ASN CA 565 200.1 136.3 66.7 73 B ASN CB 565 199.0 136.6 65.7 75 B ASN CG 565 199.5 137.5 64.6 76 B ASN OD1 565 199.7 138.7 64.8 76 B ASN ND2 565 199.7 137.0 63.4 76 B ASN C 565 199.5 135.9 68.0 71 B ASN O 565 198.8 136.7 68.6 71 B HIS N 566 199.7 134.7 68.5 68 B HIS CA 566 199.3 134.2 69.8 66 B HIS CB 566 199.9 135.1 70.9 64 B HIS CG 566 201.4 135.3 70.7 63 B HIS CD2 566 202.4 134.4 70.7 62 B HIS ND1 566 201.9 136.5 70.4 62 B HIS CE1 566 203.2 136.3 70.2 62 B HIS NE2 566 203.5 135.1 70.4 62 B HIS C 566 197.8 134.1 70.0 66 B HIS O 566 197.2 134.6 71.0 64 B LEU N 567 197.2 133.4 69.0 67 B LEU CA 567 195.8 133.1 69.0 69 B LEU CB 567 195.1 133.9 67.9 68 B LEU CG 567 195.3 135.4 68.0 68 B LEU CD1 567 194.9 136.0 66.7 68 B LEU CD2 567 194.5 135.9 69.2 68 B LEU C 567 195.7 131.6 68.8 71 B LEU O 567 196.7 131.0 68.4 71 B VAL N 568 194.5 131.0 69.0 72 B VAL CA 568 194.3 129.6 68.8 72 B VAL CB 568 193.3 129.0 69.8 71 B VAL CG1 568 193.8 127.7 70.3 71 B VAL CG2 568 193.1 130.0 71.0 71 B VAL C 568 193.8 129.5 67.3 72 B VAL O 568 193.0 130.4 66.9 73 B PRO N 569 194.4 128.6 66.5 73 B PRO CD 569 195.5 127.6 66.8 72 B PRO CA 569 193.9 128.5 65.1 72 B PRO CB 569 194.8 127.3 64.5 71 B PRO CG 569 196.0 127.4 65.4 72 B PRO C 569 192.4 128.1 65.0 71 B PRO O 569 191.9 127.2 65.7 71 B ARG N 570 191.7 128.9 64.2 70 B ARG CA 570 190.2 128.6 64.1 70 B ARG CB 570 189.4 129.5 64.9 71 B ARG CG 570 188.4 128.7 65.8 73 B ARG CD 570 187.6 129.5 66.7 74 B ARG NE 570 186.5 130.2 65.9 76 B ARG CZ 570 185.2 129.9 66.0 76 B ARG NH1 570 184.8 128.9 66.8 76 B ARG NH2 570 184.3 130.6 65.3 76 B ARG C 570 189.9 128.7 62.6 69 B ARG O 570 189.5 129.8 62.1 70 B LEU N 571 189.9 127.5 61.9 65 B LEU CA 571 189.6 127.4 60.5 61 B LEU CB 571 190.0 126.1 59.9 60 B LEU CG 571 191.4 125.9 59.4 59 B LEU CD1 571 192.5 126.2 60.4 58 B LEU CD2 571 191.6 124.5 58.8 57 B LEU C 571 188.1 127.7 60.3 59 B LEU O 571 187.3 127.0 60.9 59 B VAL N 572 187.7 128.7 59.6 57 B VAL CA 572 186.4 129.1 59.4 57 B VAL CB 572 185.9 130.3 60.3 57 B VAL CG1 572 184.4 130.6 60.1 57 B VAL CG2 572 186.3 130.0 61.7 58 B VAL C 572 186.1 129.5 57.9 55 B VAL O 572 187.0 130.1 57.3 56 B LEU N 573 185.0 129.1 57.3 53 B LEU CA 573 184.7 129.5 55.9 52 B LEU CB 573 183.9 128.3 55.3 52 B LEU CG 573 183.3 128.6 53.9 51 B LEU CD1 573 184.5 128.8 52.9 51 B LEU CD2 573 182.4 127.5 53.5 49 B LEU C 573 183.8 130.7 56.0 52 B LEU O 573 182.7 130.7 56.3 51 B GLN N 574 184.4 131.9 55.6 51 B GLN CA 574 183.7 133.2 55.6 52 B GLN CB 574 184.7 134.3 55.1 53 B GLN CG 574 186.1 134.3 55.9 57 B GLN CD 574 185.9 134.6 57.4 58 B GLN OE1 574 186.4 133.9 58.2 58 B GLN NE2 574 185.2 135.7 57.7 59 B GLN C 574 182.6 133.1 54.6 52 B GLN O 574 182.5 133.9 53.7 52 B ARG N 575 181.6 132.3 55.0 51 B ARG CA 575 180.4 132.0 54.2 52 B ARG CB 575 179.6 131.0 55.0 52 B ARG CG 575 178.4 130.4 54.2 53 B ARG CD 575 177.6 129.5 55.1 53 B ARG NE 575 178.5 128.3 55.5 53 B ARG CZ 575 178.3 127.1 55.0 54 B ARG NH1 575 177.3 126.8 54.1 54 B ARG NH2 575 179.1 126.1 55.3 54 B ARG C 575 179.6 133.3 53.9 52 B ARG O 575 179.0 133.4 52.9 51 B GLU N 576 179.4 134.2 54.9 54 B GLU CA 576 178.6 135.4 54.7 56 B GLU CB 576 178.3 136.1 56.0 59 B GLU CG 576 177.0 135.5 56.7 63 B GLU CD 576 175.8 135.4 55.7 66 B GLU OE1 576 175.5 134.3 55.2 66 B GLU OE2 576 175.2 136.5 55.4 67 B GLU C 576 179.3 136.3 53.7 55 B GLU O 576 178.7 136.8 52.8 54 B LYS N 577 180.6 136.5 54.0 54 B LYS CA 577 181.4 137.4 53.1 53 B LYS CB 577 182.9 137.5 53.7 55 B LYS CG 577 183.3 139.0 53.8 58 B LYS CD 577 182.4 139.9 54.7 59 B LYS CE 577 181.2 140.4 54.0 61 B LYS NZ 577 180.2 141.0 55.0 61 B LYS C 577 181.5 136.9 51.7 51 B LYS O 577 181.4 137.7 50.7 51 B HIS N 578 181.5 135.5 51.5 48 B HIS CA 578 181.5 134.9 50.2 44 B HIS CB 578 181.8 133.4 50.3 40 B HIS CG 578 183.2 133.1 50.8 38 B HIS CD2 578 183.7 132.0 51.4 37 B HIS ND1 578 184.2 134.0 50.8 38 B HIS CE1 578 185.3 133.4 51.3 37 B HIS NE2 578 185.1 132.2 51.7 36 B HIS C 578 180.1 135.0 49.5 43 B HIS O 578 180.0 135.2 48.3 43 B PHE N 579 179.1 134.9 50.4 43 B PHE CA 579 177.7 135.0 49.9 44 B PHE CB 579 176.7 134.7 51.0 46 B PHE CG 579 175.3 135.1 50.7 48 B PHE CD1 579 174.6 134.4 49.7 48 B PHE CD2 579 174.7 136.1 51.4 49 B PHE CE1 579 173.3 134.8 49.4 49 B PHE CE2 579 173.4 136.5 51.1 50 B PHE CZ 579 172.7 135.8 50.0 50 B PHE C 579 177.4 136.3 49.4 44 B PHE O 579 176.7 136.5 48.4 45 B HIS N 580 177.9 137.4 50.0 46 B HIS CA 580 177.7 138.7 49.6 47 B HIS CB 580 178.0 139.7 50.7 52 B HIS CG 580 177.2 139.3 52.0 55 B HIS CD2 580 175.9 139.1 52.2 56 B HIS ND1 580 177.9 139.0 53.2 57 B HIS CE1 580 177.0 138.7 54.1 57 B HIS NE2 580 175.8 138.7 53.5 57 B HIS C 580 178.4 139.1 48.3 46 B HIS O 580 178.0 139.9 47.5 46 B TYR N 581 179.5 138.4 48.1 44 B TYR CA 581 180.4 138.6 46.9 43 B TYR CB 581 181.7 137.8 47.1 43 B TYR CG 581 182.7 137.6 45.9 42 B TYR CD1 581 183.0 138.7 45.1 42 B TYR CE1 581 183.9 138.5 44.1 41 B TYR CD2 581 183.3 136.4 45.7 42 B TYR CE2 581 184.2 136.2 44.7 40 B TYR CZ 581 184.5 137.3 43.9 40 B TYR OH 581 185.4 137.1 42.9 40 B TYR C 581 179.7 137.9 45.7 42 B TYR O 581 179.4 138.6 44.6 41 B LEU N 582 179.3 136.7 45.9 41 B LEU CA 582 178.6 135.9 44.9 40 B LEU CB 582 178.3 134.5 45.4 38 B LEU CG 582 179.6 133.7 45.7 36 B LEU CD1 582 179.3 132.5 46.5 36 B LEU CD2 582 180.3 133.3 44.4 36 B LEU C 582 177.2 136.6 44.5 43 B LEU O 582 176.9 136.8 43.3 43 B LYS N 583 176.5 136.9 45.5 48 B LYS CA 583 175.2 137.5 45.4 51 B LYS CB 583 174.6 137.8 46.8 54 B LYS CG 583 173.3 138.6 46.8 59 B LYS CD 583 172.8 139.0 48.3 61 B LYS CE 583 171.6 139.9 48.2 64 B LYS NZ 583 170.9 140.2 49.5 65 B LYS C 583 175.2 138.8 44.5 51 B LYS O 583 174.2 139.1 43.8 51 B ARG N 584 176.3 139.5 44.6 52 B ARG CA 584 176.5 140.8 43.8 53 B ARG CB 584 177.6 141.6 44.5 55 B ARG CG 584 177.1 142.5 45.6 59 B ARG CD 584 176.8 143.9 45.2 61 B ARG NE 584 176.0 143.9 44.0 63 B ARG CZ 584 176.2 144.6 42.9 65 B ARG NH1 584 177.3 145.4 42.8 65 B ARG NH2 584 175.4 144.5 41.9 66 B ARG C 584 176.9 140.5 42.4 52 B ARG O 584 176.4 141.1 41.4 51 B GLY N 585 177.8 139.5 42.2 52 B GLY CA 585 178.3 139.1 40.9 49 B GLY C 585 177.2 138.5 40.0 48 B GLY O 585 177.4 138.5 38.8 47 B LEU N 586 176.2 137.9 40.6 47 B LEU CA 586 175.1 137.3 39.8 47 B LEU CB 586 174.2 136.5 40.7 46 B LEU CG 586 173.1 135.7 40.0 47 B LEU CD1 586 173.7 134.7 39.0 46 B LEU CD2 586 172.2 135.1 40.9 47 B LEU C 586 174.3 138.4 39.2 48 B LEU O 586 173.6 138.2 38.2 49 B ARG N 587 174.4 139.6 39.7 49 B ARG CA 587 173.7 140.8 39.2 48 B ARG CB 587 173.1 141.6 40.4 51 B ARG CG 587 172.6 143.0 40.1 55 B ARG CD 587 171.5 142.9 39.1 58 B ARG NE 587 171.3 144.2 38.5 62 B ARG CZ 587 171.4 144.5 37.2 64 B ARG NH1 587 171.2 145.8 36.7 65 B ARG NH2 587 171.6 143.6 36.3 65 B ARG C 587 174.4 141.7 38.3 47 B ARG O 587 173.9 142.2 37.3 45 B GLN N 588 175.7 142.0 38.6 46 B GLN CA 588 176.5 142.8 37.8 46 B GLN CB 588 176.0 144.3 37.8 46 B GLN CG 588 176.4 145.0 39.0 47 B GLN CD 588 175.9 146.4 39.1 47 B GLN OE1 588 175.1 146.8 38.3 47 B GLN NE2 588 176.3 147.1 40.1 47 B GLN C 588 178.0 142.8 38.1 46 B GLN O 588 178.4 142.6 39.3 45 B LEU N 589 178.9 143.0 37.1 45 B LEU CA 589 180.3 142.9 37.3 45 B LEU CB 589 180.9 141.7 36.6 43 B LEU CG 589 180.3 140.4 37.0 41 B LEU CD1 589 180.4 139.3 36.0 41 B LEU CD2 589 180.9 140.0 38.3 41 B LEU C 589 180.9 144.2 36.7 44 B LEU O 589 180.3 144.8 35.8 45 B THR N 590 182.1 144.6 37.2 44 B THR CA 590 182.8 145.8 36.7 45 B THR CB 590 184.0 146.1 37.7 45 B THR OG1 590 184.9 145.1 37.7 45 B THR CG2 590 183.5 146.5 39.1 45 B THR C 590 183.4 145.5 35.4 45 B THR O 590 183.4 144.4 34.9 47 B ASP N 591 184.0 146.5 34.7 45 B ASP CA 591 184.6 146.3 33.4 45 B ASP CB 591 185.0 147.7 32.8 45 B ASP CG 591 185.8 148.5 33.7 46 B ASP OD1 591 185.6 149.8 33.6 48 B ASP OD2 591 186.6 148.0 34.5 46 B ASP C 591 185.8 145.4 33.5 45 B ASP O 591 186.4 145.1 32.5 48 B ALA N 592 186.2 145.0 34.7 43 B ALA CA 592 187.3 144.1 34.9 41 B ALA CB 592 187.7 144.1 36.4 41 B ALA C 592 187.0 142.8 34.4 40 B ALA O 592 187.8 141.9 34.2 40 B TYR N 593 185.7 142.6 34.1 39 B TYR CA 593 185.1 141.3 33.6 37 B TYR CB 593 183.9 140.9 34.4 38 B TYR CG 593 184.3 140.0 35.6 38 B TYR CD1 593 184.4 140.5 36.9 37 B TYR CE1 593 184.9 139.7 37.9 37 B TYR CD2 593 184.5 138.7 35.4 38 B TYR CE2 593 185.0 137.8 36.4 38 B TYR CZ 593 185.1 138.3 37.7 37 B TYR OH 593 185.6 137.5 38.7 36 B TYR C 593 184.8 141.4 32.1 37 B TYR O 593 184.0 140.6 31.6 38 B GLU N 594 185.3 142.4 31.5 35 B GLU CA 594 185.1 142.5 30.0 34 B GLU CB 594 185.7 143.8 29.5 35 B GLU CG 594 184.9 145.1 29.8 37 B GLU CD 594 185.6 146.4 29.4 38 B GLU OE1 594 184.9 147.4 29.2 39 B GLU OE2 594 186.9 146.4 29.3 39 B GLU C 594 185.8 141.3 29.3 32 B GLU O 594 185.4 141.0 28.2 31 B CYS N 595 186.8 140.8 30.0 32 B CYS CA 595 187.6 139.6 29.5 31 B CYS CB 595 188.9 139.5 30.2 31 B CYS SG 595 188.9 139.1 32.0 33 B CYS C 595 186.9 138.3 29.5 29 B CYS O 595 187.4 137.3 28.9 27 B LEU N 596 185.8 138.2 30.2 28 B LEU CA 596 184.9 137.0 30.3 27 B LEU CB 596 184.8 136.6 31.8 26 B LEU CG 596 186.0 135.8 32.3 26 B LEU CD1 596 185.8 135.6 33.8 27 B LEU CD2 596 186.2 134.5 31.6 25 B LEU C 596 183.6 137.3 29.7 28 B LEU O 596 182.6 136.7 30.1 28 B ASP N 597 183.6 138.3 28.8 29 B ASP CA 597 182.4 138.8 28.1 29 B ASP CB 597 182.7 140.0 27.4 30 B ASP CG 597 181.5 140.6 26.7 31 B ASP OD1 597 180.4 140.6 27.3 32 B ASP OD2 597 181.6 141.0 25.5 32 B ASP C 597 181.8 137.7 27.1 29 B ASP O 597 180.7 137.8 26.6 29 B ALA N 598 182.6 136.7 26.9 28 B ALA CA 598 182.2 135.6 26.0 26 B ALA CB 598 183.3 135.4 24.9 25 B ALA C 598 182.1 134.3 26.8 25 B ALA O 598 182.0 133.2 26.3 23 B SER N 599 182.0 134.4 28.2 26 B SER CA 599 181.9 133.3 29.1 27 B SER CB 599 183.2 133.1 29.9 28 B SER OG 599 184.3 133.0 29.0 33 B SER C 599 180.8 133.6 30.1 27 B SER O 599 180.9 133.3 31.3 28 B ARG N 600 179.7 134.3 29.7 25 B ARG CA 600 178.7 134.6 30.6 25 B ARG CB 600 177.8 135.8 30.1 24 B ARG CG 600 178.7 137.0 30.0 25 B ARG CD 600 178.0 138.2 29.4 25 B ARG NE 600 177.0 138.7 30.2 27 B ARG CZ 600 176.0 139.4 29.8 27 B ARG NH1 600 175.9 139.8 28.5 28 B ARG NH2 600 175.0 139.8 30.6 28 B ARG C 600 177.9 133.4 31.2 26 B ARG O 600 177.5 133.5 32.4 27 B PRO N 601 177.7 132.4 30.5 26 B PRO CD 601 177.7 132.2 29.0 26 B PRO CA 601 176.9 131.3 31.1 26 B PRO CB 601 176.7 130.3 30.0 25 B PRO CG 601 176.5 131.2 28.8 25 B PRO C 601 177.8 130.7 32.2 27 B PRO O 601 177.4 130.0 33.1 30 B TRP N 602 179.1 130.9 32.1 27 B TRP CA 602 180.1 130.4 33.0 26 B TRP CB 602 181.5 130.6 32.6 24 B TRP CG 602 182.0 129.4 31.7 23 B TRP CD2 602 182.3 128.1 32.1 23 B TRP CE2 602 182.7 127.4 30.9 21 B TRP CE3 602 182.3 127.4 33.3 22 B TRP CD1 602 182.2 129.5 30.3 22 B TRP NE1 602 182.6 128.3 29.9 22 B TRP CZ2 602 183.1 126.1 30.9 21 B TRP CZ3 602 182.7 126.1 33.3 22 B TRP CH2 602 183.1 125.4 32.1 21 B TRP C 602 179.9 131.2 34.3 29 B TRP O 602 179.9 130.6 35.4 31 B LEU N 603 179.7 132.5 34.2 30 B LEU CA 603 179.6 133.3 35.4 31 B LEU CB 603 179.6 134.8 35.1 31 B LEU CG 603 181.1 135.1 34.6 32 B LEU CD1 603 181.1 136.4 33.8 31 B LEU CD2 603 182.0 135.2 35.9 32 B LEU C 603 178.3 132.9 36.1 33 B LEU O 603 178.3 132.8 37.4 35 B CYS N 604 177.2 132.5 35.4 33 B CYS CA 604 176.0 132.1 36.0 32 B CYS CB 604 174.9 131.8 35.0 32 B CYS SG 604 174.4 133.2 34.0 36 B CYS C 604 176.3 130.8 36.8 33 B CYS O 604 176.0 130.6 38.0 35 B TYR N 605 177.0 129.8 36.1 31 B TYR CA 605 177.3 128.5 36.7 29 B TYR CB 605 177.9 127.6 35.6 29 B TYR CG 605 178.5 126.3 36.3 28 B TYR CD1 605 177.7 125.3 36.9 28 B TYR CE1 605 178.2 124.3 37.6 25 B TYR CD2 605 179.9 126.1 36.3 26 B TYR CE2 605 180.4 125.1 37.0 25 B TYR CZ 605 179.6 124.1 37.6 25 B TYR OH 605 180.2 123.1 38.2 27 B TYR C 605 178.2 128.7 37.9 29 B TYR O 605 177.9 128.1 38.9 31 B TRP N 606 179.3 129.3 37.8 30 B TRP CA 606 180.2 129.5 38.9 31 B TRP CB 606 181.4 130.3 38.6 31 B TRP CG 606 182.3 129.8 37.5 30 B TRP CD2 606 183.0 130.6 36.5 30 B TRP CE2 606 183.7 129.6 35.7 30 B TRP CE3 606 183.1 131.9 36.2 31 B TRP CD1 606 182.7 128.5 37.2 30 B TRP NE1 606 183.5 128.4 36.1 30 B TRP CZ2 606 184.5 130.1 34.6 30 B TRP CZ3 606 183.9 132.3 35.1 30 B TRP CH2 606 184.6 131.4 34.3 30 B TRP C 606 179.6 130.1 40.2 32 B TRP O 606 179.7 129.6 41.3 33 B ILE N 607 178.8 131.1 40.0 32 B ILE CA 607 178.1 131.8 41.0 32 B ILE CB 607 177.6 133.2 40.6 32 B ILE CG2 607 176.6 133.8 41.5 32 B ILE CG1 607 178.8 134.1 40.3 30 B ILE CD1 607 178.4 135.3 39.5 30 B ILE C 607 177.0 131.0 41.6 32 B ILE O 607 176.9 130.7 42.8 33 B LEU N 608 176.1 130.5 40.7 31 B LEU CA 608 174.9 129.6 41.1 29 B LEU CB 608 174.1 129.4 39.9 29 B LEU CG 608 172.7 130.0 39.8 30 B LEU CD1 608 172.8 131.5 40.0 30 B LEU CD2 608 172.1 129.7 38.4 31 B LEU C 608 175.4 128.3 41.6 30 B LEU O 608 174.5 127.5 41.9 31 B HIS N 609 176.6 128.0 41.6 29 B HIS CA 609 177.1 126.7 42.1 29 B HIS CB 609 178.0 126.0 41.1 27 B HIS CG 609 178.5 124.6 41.6 25 B HIS CD2 609 179.7 124.2 41.8 24 B HIS ND1 609 177.6 123.7 42.1 25 B HIS CE1 609 178.3 122.7 42.5 25 B HIS NE2 609 179.6 122.9 42.4 24 B HIS C 609 177.7 126.9 43.4 31 B HIS O 609 177.8 126.0 44.3 32 B SER N 610 178.4 128.1 43.6 34 B SER CA 610 179.0 128.4 44.8 36 B SER CB 610 179.9 129.6 44.6 35 B SER OG 610 180.9 129.4 43.6 34 B SER C 610 177.9 128.6 45.9 37 B SER O 610 177.9 128.1 47.0 37 B LEU N 611 176.9 129.4 45.4 38 B LEU CA 611 175.7 129.6 46.3 39 B LEU CB 611 174.7 130.5 45.6 37 B LEU CG 611 175.2 131.9 45.1 37 B LEU CD1 611 174.2 132.6 44.2 35 B LEU CD2 611 175.6 132.7 46.4 36 B LEU C 611 175.1 128.3 46.6 41 B LEU O 611 174.7 128.1 47.7 43 B GLU N 612 175.0 127.4 45.6 42 B GLU CA 612 174.5 126.1 45.8 44 B GLU CB 612 174.5 125.3 44.4 44 B GLU CG 612 173.9 123.9 44.5 45 B GLU CD 612 174.6 123.0 43.6 46 B GLU OE1 612 175.2 122.0 44.1 46 B GLU OE2 612 174.7 123.2 42.3 45 B GLU C 612 175.2 125.3 46.8 45 B GLU O 612 174.7 124.5 47.5 46 B LEU N 613 176.5 125.5 46.8 46 B LEU CA 613 177.3 124.7 47.8 48 B LEU CB 613 178.8 124.7 47.3 48 B LEU CG 613 179.1 123.6 46.3 47 B LEU CD1 613 180.1 124.2 45.3 47 B LEU CD2 613 179.8 122.4 46.9 48 B LEU C 613 177.3 125.3 49.2 49 B LEU O 613 177.3 124.6 50.2 49 B LEU N 614 177.1 126.7 49.2 50 B LEU CA 614 177.1 127.4 50.5 51 B LEU CB 614 177.5 128.9 50.3 48 B LEU CG 614 178.9 129.1 49.8 46 B LEU CD1 614 179.1 130.5 49.4 44 B LEU CD2 614 179.9 128.7 50.9 44 B LEU C 614 175.7 127.3 51.1 54 B LEU O 614 175.3 127.9 52.1 55 B ASP N 615 174.8 126.5 50.4 57 B ASP CA 615 173.5 126.3 50.8 60 B ASP CB 615 173.4 125.6 52.2 61 B ASP CG 615 172.1 125.0 52.5 62 B ASP OD1 615 171.2 125.0 51.7 63 B ASP OD2 615 172.0 124.5 53.7 63 B ASP C 615 172.7 127.6 50.8 61 B ASP O 615 171.7 127.7 51.6 62 B GLU N 616 173.1 128.5 50.0 63 B GLU CA 616 172.4 129.8 49.9 65 B GLU CB 616 173.4 130.9 49.5 65 B GLU CG 616 174.6 131.0 50.6 66 B GLU CD 616 174.2 131.8 51.8 67 B GLU OE1 616 173.1 132.4 51.9 66 B GLU OE2 616 175.0 131.8 52.8 67 B GLU C 616 171.2 129.7 48.9 66 B GLU O 616 171.2 128.8 48.2 67 B PRO N 617 170.3 130.7 49.0 68 B PRO CD 617 170.4 131.8 49.9 70 B PRO CA 617 169.1 130.8 48.2 69 B PRO CB 617 168.3 131.8 49.0 70 B PRO CG 617 169.3 132.8 49.4 71 B PRO C 617 169.2 131.3 46.8 69 B PRO O 617 170.1 132.1 46.5 71 B ILE N 618 168.3 130.8 45.9 69 B ILE CA 618 168.3 131.2 44.5 69 B ILE CB 618 168.6 130.0 43.6 68 B ILE CG2 618 168.8 130.5 42.1 67 B ILE CG1 618 169.8 129.1 44.1 68 B ILE CD1 618 171.1 129.8 44.3 67 B ILE C 618 166.9 131.7 44.2 68 B ILE O 618 166.1 131.0 43.6 70 B PRO N 619 166.6 133.0 44.7 68 B PRO CD 619 167.6 133.9 45.3 67 B PRO CA 619 165.3 133.7 44.5 67 B PRO CB 619 165.7 135.1 44.5 67 B PRO CG 619 166.8 135.1 45.6 67 B PRO C 619 164.5 133.3 43.2 67 B PRO O 619 165.0 133.4 42.1 68 B GLN N 620 163.3 132.9 43.4 68 B GLN CA 620 162.4 132.5 42.4 69 B GLN CB 620 161.0 132.2 42.9 71 B GLN CG 620 160.9 131.1 44.0 73 B GLN CD 620 159.6 130.5 44.3 74 B GLN OE1 620 158.5 131.0 43.9 75 B GLN NE2 620 159.6 129.3 45.0 74 B GLN C 620 162.3 133.5 41.2 68 B GLN O 620 161.7 133.1 40.2 68 B ILE N 621 162.8 134.7 41.4 66 B ILE CA 621 162.8 135.7 40.4 65 B ILE CB 621 162.4 137.1 41.0 66 B ILE CG2 621 162.1 138.1 39.9 65 B ILE CG1 621 161.3 137.0 42.0 67 B ILE CD1 621 161.6 136.5 43.4 67 B ILE C 621 164.2 135.8 39.7 63 B ILE O 621 164.2 136.0 38.5 62 B VAL N 622 165.2 135.7 40.5 60 B VAL CA 622 166.6 135.7 39.9 59 B VAL CB 622 167.6 135.8 41.0 59 B VAL CG1 622 167.8 134.4 41.7 59 B VAL CG2 622 168.9 136.2 40.4 60 B VAL C 622 166.8 134.5 39.0 57 B VAL O 622 167.4 134.6 37.9 56 B ALA N 623 166.4 133.3 39.5 56 B ALA CA 623 166.5 132.1 38.7 54 B ALA CB 623 165.9 131.0 39.5 54 B ALA C 623 165.8 132.2 37.4 54 B ALA O 623 166.3 131.8 36.4 54 B THR N 624 164.7 132.9 37.4 52 B THR CA 624 164.0 133.2 36.2 52 B THR CB 624 162.6 133.8 36.4 53 B THR OG1 624 161.8 132.9 37.2 55 B THR CG2 624 161.9 134.2 35.1 53 B THR C 624 164.8 134.0 35.2 52 B THR O 624 164.9 133.7 34.1 52 B ASP N 625 165.3 135.1 35.7 52 B ASP CA 625 166.1 136.0 34.9 51 B ASP CB 625 166.7 137.2 35.7 53 B ASP CG 625 165.6 138.0 36.4 54 B ASP OD1 625 164.6 138.3 35.8 53 B ASP OD2 625 165.8 138.3 37.6 55 B ASP C 625 167.3 135.2 34.3 49 B ASP O 625 167.5 135.3 33.1 49 B VAL N 626 167.9 134.4 35.1 46 B VAL CA 626 169.0 133.6 34.7 44 B VAL CB 626 169.6 132.6 31.7 42 B VAL CG1 626 170.6 131.7 35.1 40 B VAL CG2 626 170.3 133.5 36.8 41 B VAL C 626 168.5 132.7 33.5 44 B VAL O 626 169.1 132.6 32.5 44 B CYS N 627 167.3 132.1 33.7 44 B CYS CA 627 166.7 131.3 32.7 44 B CYS CB 627 165.4 130.6 33.1 44 B CYS SG 627 165.5 129.4 34.4 45 B CYS C 627 166.4 132.0 31.4 45 B CYS O 627 166.6 131.5 30.3 45 B GLN N 628 166.0 133.3 31.6 47 B GLN CA 628 165.6 134.2 30.5 48 B GLN CB 628 164.8 135.3 31.1 52 B GLN CG 628 164.6 136.6 30.1 57 B GLN CD 628 163.7 137.6 30.8 60 B GLN OE1 628 162.6 137.9 30.3 62 B GLN NE2 628 164.2 138.2 31.9 61 B GLN C 628 166.8 134.7 29.8 46 B GLN O 628 166.8 134.9 28.6 46 B PHE N 629 167.9 134.8 30.5 43 B PHE CA 629 169.2 135.3 30.0 41 B PHE CB 629 170.1 135.8 31.1 39 B PHE CG 629 171.5 136.1 30.6 39 B PHE CD1 629 171.7 137.1 29.6 40 B PHE CD2 629 172.6 135.4 31.0 39 B PHE CE1 629 173.0 137.4 29.1 39 B PHE CE2 629 173.9 135.7 30.5 38 B PHE CZ 629 174.1 136.7 29.5 38 B PHE C 629 169.8 134.2 29.1 40 B PHE O 629 170.2 134.4 28.0 40 B LEU N 630 169.9 133.0 29.7 39 B LEU CA 630 170.5 131.8 29.0 36 B LEU CB 630 170.5 130.6 30.0 33 B LEU CG 630 171.4 130.7 31.2 31 B LEU CD1 630 171.4 129.4 32.0 30 B LEU CD2 630 172.8 131.0 30.7 31 B LEU C 630 169.7 131.5 27.7 38 B LEU O 630 170.3 131.1 26.7 38 B GLU N 631 168.4 131.8 27.7 39 B GLU CA 631 167.6 131.6 26.6 42 B GLU CB 631 166.1 131.9 26.9 46 B GLU CG 631 165.1 131.3 26.0 52 B GLU CD 631 163.7 131.0 26.8 56 B GLU OE1 631 163.0 130.1 26.3 58 B GLU OE2 631 163.4 131.8 27.7 57 B GLU C 631 168.1 132.5 25.4 42 B GLU O 631 168.0 132.2 24.3 42 B LEU N 632 168.6 133.7 25.8 42 B LEU CA 632 169.2 134.7 24.9 42 B LEU CB 632 169.3 136.0 25.6 42 B LEU CG 632 168.0 136.8 25.8 42 B LEU CD1 632 168.0 137.8 27.0 42 B LEU CD2 632 167.6 137.5 24.5 41 B LEU C 632 170.6 134.3 24.4 42 B LEU O 632 171.0 134.7 23.4 42 B CYS N 633 171.3 133.5 25.2 42 B CYS CA 633 172.6 132.9 24.9 42 B CYS CB 633 173.3 132.5 26.2 40 B CYS SG 633 173.8 133.8 27.2 40 B CYS C 633 172.5 131.8 23.9 43 B CYS O 633 173.3 131.6 23.1 44 B GLN N 634 171.4 131.0 24.1 43 B GLN CA 634 171.1 129.8 23.3 43 B GLN CB 634 169.9 129.1 23.7 42 B GLN CG 634 169.6 127.7 23.2 41 B GLN CD 634 168.5 127.0 23.9 41 B GLN OE1 634 168.6 125.8 24.1 41 B GLN NE2 634 167.5 127.7 24.2 41 B GLN C 634 171.0 130.1 21.8 43 B GLN O 634 170.4 131.1 21.4 43 B SER N 635 171.6 129.3 20.9 44 B SER CA 635 171.6 129.5 19.5 45 B SER CB 635 173.0 129.0 18.9 44 B SER OG 635 173.0 129.1 17.5 44 B SER C 635 170.5 128.7 18.7 47 B SER O 635 170.0 127.7 19.2 47 B PRO N 636 170.0 129.4 17.7 47 B PRO CD 636 170.3 130.7 17.2 47 B PRO CA 636 168.9 128.7 16.9 48 B PRO CB 636 168.5 129.8 15.9 48 B PRO CG 636 169.8 130.6 15.7 48 B PRO C 636 169.4 127.4 16.2 49 B PRO O 636 168.7 126.6 15.7 50 B ASP N 637 170.7 127.2 16.3 48 B ASP CA 637 171.3 126.0 15.7 47 B ASP CB 637 172.7 126.4 15.0 50 B ASP CG 637 172.4 127.3 13.8 53 B ASP OD1 637 171.4 127.1 13.1 54 B ASP OD2 637 173.3 128.2 13.6 53 B ASP C 637 171.6 125.0 16.9 46 B ASP O 637 172.1 123.9 16.6 46 B GLY N 638 171.2 125.4 18.1 43 B GLY CA 638 171.4 124.6 19.2 39 B GLY C 638 172.6 124.9 20.0 38 B GLY O 638 173.6 125.5 19.5 38 B GLY N 639 172.6 124.6 21.3 37 B GLY CA 639 173.8 124.9 22.1 35 B GLY C 639 173.7 126.4 22.6 34 B GLY O 639 172.8 127.1 22.4 33 B PHE N 640 174.8 126.8 23.4 33 B PHE CA 640 174.8 128.1 23.9 34 B PHE CB 640 174.7 128.1 25.4 35 B PHE CG 640 173.4 127.5 25.9 36 B PHE CD1 640 173.2 126.2 25.9 38 B PHE CD2 640 172.3 128.4 26.2 37 B PHE CE1 640 171.9 125.6 26.3 39 B PHE CE2 640 171.1 127.9 26.6 38 B PHE CZ 640 170.9 126.5 26.6 40 B PHE C 640 176.0 128.9 23.6 33 B PHE O 640 177.1 128.4 23.5 34 B GLY N 641 175.8 130.3 23.4 31 B GLY CA 641 177.0 131.1 23.1 31 B GLY C 641 177.5 131.7 24.4 32 B GLY O 641 177.0 131.4 25.5 33 B GLY N 642 178.5 132.6 24.3 33 B GLY CA 642 179.1 133.2 25.6 33 B GLY C 642 178.3 134.4 26.1 32 B GLY O 642 178.6 134.9 27.2 32 B GLY N 643 177.3 134.8 25.3 32 B GLY CA 643 176.5 135.9 25.7 31 B GLY C 643 175.4 136.0 24.6 32 B GLY O 643 175.4 135.3 23.6 32 B PRO N 644 174.4 137.0 24.8 32 B PRO CD 644 174.1 137.9 25.9 32 B PRO CA 644 173.4 137.1 23.7 32 B PRO CB 644 172.6 138.3 24.2 32 B PRO CG 644 172.7 138.2 25.7 31 B PRO C 644 174.0 137.3 22.4 31 B PRO O 644 174.9 138.1 22.2 33 B GLY N 645 173.6 136.4 21.4 32 B GLY CA 645 174.1 136.6 20.1 33 B GLY C 645 175.4 136.0 19.7 35 B GLY O 645 175.9 136.2 18.5 37 B GLN N 646 176.1 135.2 20.6 33 B GLN CA 646 177.4 134.6 20.2 32 B GLN CB 646 178.3 134.6 21.5 31 B GLN CG 646 178.7 136.0 21.9 29 B GLN CD 646 179.4 136.0 23.2 27 B GLN OE1 646 179.1 136.9 24.0 29 B GLN NE2 646 180.3 135.1 23.4 27 B GLN C 646 177.2 133.2 19.7 32 B GLN O 646 176.3 132.5 20.2 33 B TYR N 647 178.0 132.8 18.8 30 B TYR CA 647 178.0 131.5 18.2 29 B TYR CB 647 179.2 131.3 17.3 28 B TYR CG 647 179.2 132.2 16.1 29 B TYR CD1 647 180.3 132.4 15.3 29 B TYR CE1 647 180.2 133.2 14.2 30 B TYR CD2 647 178.0 133.0 15.8 29 B TYR CE2 647 178.0 133.8 14.7 29 B TYR CZ 647 179.0 133.9 13.9 30 B TYR OH 647 178.9 134.7 12.8 33 B TYR C 647 178.1 130.4 19.3 29 B TYR O 647 178.9 130.6 20.3 30 B PRO N 648 177.3 129.4 19.3 28 B PRO CD 648 176.4 128.9 18.2 27 B PRO CA 648 177.3 128.3 20.3 25 B PRO CB 648 176.3 127.3 19.8 25 B PRO CG 648 176.4 127.4 18.4 26 B PRO C 648 178.7 127.8 20.5 24 B PRO O 648 179.4 127.7 19.5 27 B HIS N 649 179.0 127.3 21.7 21 B HIS CA 649 180.4 126.8 21.9 19 B HIS CB 649 181.3 128.0 22.4 18 B HIS CG 649 182.7 127.6 22.6 15 B HIS CD2 649 183.8 128.1 22.0 14 B HIS ND1 649 183.1 126.8 23.7 14 B HIS CE1 649 184.4 126.8 23.7 13 B HIS NE2 649 184.9 127.6 22.7 12 B HIS C 649 180.1 125.8 23.0 20 B HIS O 649 179.3 126.0 23.9 21 B LEU N 650 180.8 124.7 23.0 21 B LEU CA 650 180.6 123.6 24.0 21 B LEU CB 650 181.4 122.3 23.6 20 B LEU CG 650 180.7 121.4 22.6 19 B LEU CD1 650 181.6 120.2 22.4 18 B LEU CD2 650 179.4 120.9 23.1 18 B LEU C 650 180.9 124.0 25.4 23 B LEU O 650 180.3 123.5 26.4 24 B ALA N 651 181.9 124.9 25.7 24 B ALA CA 651 182.2 125.3 27.1 25 B ALA CB 651 183.5 126.1 27.2 23 B ALA C 651 181.0 126.1 27.7 26 B ALA O 651 180.5 125.7 28.8 25 B PRO N 652 180.4 127.1 27.0 26 B PRO CD 652 181.0 127.8 25.8 27 B PRO CA 652 179.3 127.9 27.5 27 B PRO CB 652 179.1 129.0 26.4 27 B PRO CG 652 180.4 129.2 25.9 27 B PRO C 652 178.0 126.9 27.6 28 B PRO O 652 177.1 127.1 28.4 29 B THR N 653 177.9 126.0 26.6 26 B THR CA 653 176.8 125.0 26.5 24 B THR CB 653 176.9 124.1 25.3 23 B THR OG1 653 176.8 124.9 24.1 21 B THR CG2 653 175.8 123.0 25.3 23 B THR C 653 176.8 124.1 27.8 23 B THR O 653 175.8 123.9 28.5 24 B TYR N 654 178.0 123.6 28.1 23 B TYR CA 654 178.2 122.8 29.3 22 B TYR CB 654 179.6 122.4 29.5 19 B TYR CG 654 180.0 122.0 30.9 18 B TYR CD1 654 179.8 120.7 31.3 17 B TYR CE1 654 180.2 120.2 32.5 17 B TYR CD2 654 180.6 122.9 31.8 18 B TYR CE2 654 181.0 122.4 33.1 17 B TYR CZ 654 180.8 121.1 33.4 18 B TYR OH 654 181.2 120.7 34.7 19 B TYR C 654 177.7 123.6 30.5 24 B TYR O 654 177.0 123.2 31.4 25 B ALA N 655 178.2 124.9 30.6 27 B ALA CA 655 177.9 125.8 31.7 27 B ALA CB 655 178.7 127.0 31.6 26 B ALA C 655 176.4 126.1 31.8 27 B ALA O 655 175.8 126.0 32.9 27 B ALA N 656 175.8 126.5 30.7 27 B ALA CA 656 174.4 126.8 30.6 28 B ALA CB 656 174.0 127.2 29.2 27 B ALA C 656 173.6 125.7 31.2 30 B ALA O 656 172.7 125.8 32.0 32 B VAL N 657 173.8 124.5 30.6 31 B VAL CA 657 173.1 123.3 31.1 31 B VAL CB 657 173.4 122.0 30.2 30 B VAL CG1 657 172.6 120.8 30.6 29 B VAL CG2 657 173.2 122.3 28.8 29 B VAL C 657 173.2 123.0 32.6 32 B VAL O 657 172.3 122.8 33.2 33 B ASN N 658 174.5 123.1 33.1 32 B ASN CA 658 174.7 122.9 34.5 31 B ASN CB 658 176.2 122.9 34.8 30 B ASN CG 658 176.7 121.6 34.9 30 B ASN OD1 658 176.1 120.6 34.5 31 B ASN ND2 658 177.9 121.4 35.5 30 B ASN C 658 173.9 124.0 35.3 33 B ASN O 658 173.3 123.6 36.3 33 B ALA N 659 173.9 125.2 34.8 34 B ALA CA 659 173.2 126.3 35.5 34 B ALA CB 659 173.4 127.6 34.8 33 B ALA C 659 171.7 125.9 35.6 35 B ALA O 659 171.2 125.7 36.7 34 B LEU N 660 171.1 125.8 34.4 35 B LEU CA 660 169.7 125.4 34.3 35 B LEU CB 660 169.4 125.1 32.9 35 B LEU CG 660 169.4 126.3 31.9 36 B LEU CD1 660 169.2 125.8 30.5 36 B LEU CD2 660 168.3 127.2 32.3 35 B LEU C 660 169.3 124.2 35.2 37 B LEU O 660 168.2 124.2 35.8 38 B CYS N 661 170.2 123.2 35.4 38 B CYS CA 661 169.9 122.1 36.3 39 B CYS CB 661 170.8 120.9 35.9 39 B CYS SG 661 170.4 120.1 34.4 39 B CYS C 661 170.0 122.5 37.7 40 B CYS O 661 169.3 121.9 38.6 42 B ILE N 662 171.0 123.4 38.1 41 B ILE CA 662 171.1 123.8 39.5 40 B ILE CB 662 172.3 124.8 39.6 39 B ILE CG2 662 172.4 125.3 41.1 38 B ILE CG1 662 173.6 124.0 39.3 38 B ILE CD1 662 174.9 124.9 39.6 37 B ILE C 662 169.8 124.4 39.9 41 B ILE O 662 169.3 124.2 41.0 40 B ILE N 663 169.2 125.3 39.0 42 B ILE CA 663 168.0 125.9 39.3 44 B ILE CB 663 167.5 126.8 38.2 44 B ILE CG2 663 166.1 127.4 38.5 44 B ILE CG1 663 168.5 128.0 38.1 44 B ILE CD1 663 168.3 128.9 36.9 43 B ILE C 663 167.0 124.7 39.4 47 B ILE O 663 166.5 124.3 40.4 49 B GLY N 664 166.9 123.9 38.3 48 B GLY CA 664 166.1 122.7 38.2 49 B GLY C 664 164.5 122.9 38.3 50 B GLY O 664 163.9 122.3 39.2 51 B THR N 665 163.9 123.5 37.4 49 B THR CA 665 162.5 123.7 37.4 48 B THR CB 665 162.2 125.2 37.7 48 B THR OG1 665 162.6 126.0 36.6 48 B THR CG2 665 162.9 125.6 39.0 48 B THR C 665 162.0 123.5 36.0 50 B THR O 665 162.7 123.7 35.0 50 B GLU N 666 160.7 123.2 35.9 51 B GLU CA 666 160.1 123.0 34.5 53 B GLU CB 666 158.6 123.1 34.6 56 B GLU CG 666 157.9 121.8 35.0 59 B GLU CD 666 158.4 120.6 34.2 61 B GLU OE1 666 159.0 119.7 34.9 62 B GLU OE2 666 158.3 120.5 33.0 61 B GLU C 666 160.6 124.1 33.6 53 B GLU O 666 160.9 123.8 32.4 53 B GLU N 667 160.6 125.4 34.0 52 B GLU CA 667 161.0 126.5 33.3 51 B GLU CB 667 160.9 127.8 34.1 53 B GLU CG 667 161.4 129.0 33.3 54 B GLU CD 667 161.4 130.3 34.2 55 B GLU OE1 667 161.7 130.1 35.4 55 B GLU OE2 667 161.2 131.4 33.7 55 B GLU C 667 162.5 126.4 32.8 50 B GLU O 667 162.7 126.5 31.6 50 B ALA N 668 163.4 126.2 33.7 47 B ALA CA 668 164.8 126.1 33.4 46 B ALA CB 668 165.6 125.9 34.7 46 B ALA C 668 165.1 125.0 32.4 46 B ALA O 668 165.6 125.2 31.3 47 B TYR N 669 164.6 123.8 32.8 44 B TYR CA 669 164.8 122.6 31.9 43 B TYR CB 669 164.0 121.4 32.5 41 B TYR CG 669 164.5 120.9 33.8 39 B TYR CD1 669 163.6 120.2 34.7 39 B TYR CE1 669 164.0 119.7 35.9 38 B TYR CD2 669 165.8 120.9 34.2 39 B TYR CE2 669 166.2 120.4 35.4 39 B TYR CZ 669 165.3 119.8 36.2 38 B TYR OH 669 165.7 119.3 37.4 37 B TYR C 669 164.2 122.9 30.6 44 B TYR O 669 164.8 122.5 29.5 45 B ASN N 670 163.0 123.6 30.5 43 B ASN CA 670 162.4 123.9 29.3 44 B ASN CB 670 160.9 124.3 29.5 47 B ASN CG 670 160.0 123.2 29.8 49 B ASN OD1 670 160.4 122.0 29.9 51 B ASN ND2 670 158.7 123.5 30.0 51 B ASN C 670 163.1 124.9 28.4 45 B ASN O 670 162.7 125.1 27.2 46 B VAL N 671 164.1 125.6 28.9 43 B VAL CA 671 164.9 126.5 28.1 40 B VAL CB 671 165.9 127.4 29.0 40 B VAL CG1 671 166.7 128.3 28.1 39 B VAL CG2 671 165.1 128.2 30.0 40 B VAL C 671 165.8 125.8 27.1 40 B VAL O 671 165.9 126.2 25.9 40 B ILE N 672 166.3 124.6 27.5 39 B ILE CA 672 167.1 123.7 26.7 37 B ILE CB 672 167.7 122.6 27.6 34 B ILE CG2 672 168.8 121.9 26.8 34 B ILE CG1 672 168.3 123.1 28.9 32 B ILE CD1 672 168.8 122.1 29.8 29 B ILE C 672 166.4 123.0 25.5 39 B ILE O 672 165.5 122.2 25.7 40 B ASN N 673 166.8 123.4 24.3 39 B ASN CA 673 166.2 122.8 23.1 39 B ASN CB 673 166.3 123.8 21.9 39 B ASN CG 673 165.8 123.2 20.6 41 B ASN OD1 673 165.7 122.0 20.4 41 B ASN ND2 673 165.4 124.2 19.8 40 B ASN C 673 167.0 121.5 22.8 39 B ASN O 673 168.1 121.6 22.1 38 B ARG N 674 166.5 120.4 23.2 40 B ARG CA 674 167.1 119.1 23.0 40 B ARG CB 674 166.3 118.1 23.8 38 B ARG CG 674 166.3 118.3 25.3 37 B ARG CD 674 165.3 117.3 25.9 38 B ARG NE 674 165.7 115.9 25.7 38 B ARG CZ 674 165.1 115.0 24.9 37 B ARG NH1 674 164.0 115.3 24.2 38 B ARG NH2 674 165.5 113.8 24.9 37 B ARG C 674 167.2 118.5 21.6 41 B ARG O 674 168.1 117.7 21.3 41 B GLU N 675 166.3 119.0 20.7 44 B GLU CA 675 166.3 118.5 19.3 47 B GLU CB 675 164.9 118.7 18.6 51 B GLU CG 675 163.9 119.7 19.3 57 B GLU CD 675 163.4 119.1 20.7 59 B GLU OE1 675 163.5 119.8 21.7 60 B GLU OE2 675 162.8 118.0 20.7 61 B GLU C 675 167.4 119.3 18.6 46 B GLU O 675 168.0 118.8 17.6 47 B LYS N 676 167.6 120.5 19.0 44 B LYS CA 676 168.6 121.4 18.4 41 B LYS CB 676 168.3 122.8 18.6 42 B LYS CG 676 167.4 123.3 17.5 45 B LYS CD 676 168.1 123.4 16.2 47 B LYS CE 676 167.2 123.8 15.1 50 B LYS NZ 676 166.4 125.0 15.4 52 B LYS C 676 170.0 121.1 19.0 39 B LYS O 676 171.0 121.2 18.3 38 B LEU N 677 170.0 120.7 20.2 35 B LEU CA 677 171.3 120.4 20.9 33 B LEU CB 677 171.0 120.1 22.4 31 B LEU CG 677 172.2 119.9 23.4 29 B LEU CD1 677 173.2 121.0 23.3 29 B LEU CD2 677 171.6 119.9 24.8 28 B LEU C 677 172.0 119.1 20.3 34 B LEU O 677 173.2 119.1 20.2 34 B LEU N 678 171.2 118.2 19.8 34 B LEU CA 678 171.7 117.0 19.2 34 B LEU CB 678 170.7 115.9 19.0 35 B LEU CG 678 170.8 114.6 19.7 35 B LEU CD1 678 169.9 113.5 19.1 35 B LEU CD2 678 172.2 114.1 19.6 35 B LEU C 678 172.3 117.4 17.8 35 B LEU O 678 173.4 117.0 17.5 35 B GLN N 679 171.6 118.2 17.1 36 B GLN CA 679 172.1 118.7 15.8 39 B GLN CB 679 171.2 119.8 15.2 42 B GLN CG 679 169.9 119.4 14.7 47 B GLN CD 679 169.0 120.6 14.3 50 B GLN OE1 679 169.5 121.7 14.0 51 B GLN NE2 679 167.7 120.4 14.6 52 B GLN C 679 173.4 119.3 16.0 38 B GLN O 679 174.4 119.0 15.2 39 B TYR N 680 173.5 120.2 16.9 37 B TYR CA 680 174.8 120.9 17.3 34 B TYR CB 680 174.5 121.9 18.4 33 B TYR CG 680 175.7 122.6 18.9 31 B TYR CD1 680 176.5 123.4 18.0 31 B TYR CE1 680 177.6 124.0 18.4 31 B TYR CD2 680 176.2 122.5 20.2 31 B TYR CE2 680 177.3 123.1 20.6 30 B TYR CZ 680 178.0 123.8 19.7 30 B TYR OH 680 179.2 124.4 20.2 32 B TYR C 680 175.8 120.0 17.6 33 B TYR O 680 176.9 120.0 17.1 33 B LEU N 681 175.6 119.1 18.6 31 B LEU CA 681 176.5 118.1 19.0 30 B LEU CB 681 176.0 117.1 20.0 28 B LEU CG 681 175.7 117.6 21.4 26 B LEU CD1 681 175.4 116.5 22.4 26 B LEU CD2 681 176.9 118.4 21.8 25 B LEU C 681 177.0 117.3 17.8 31 B LEU O 681 178.2 117.0 17.7 33 B TYR N 682 176.1 116.9 16.9 31 B TYR CA 682 176.5 116.2 15.8 33 B TYR CB 682 175.3 115.6 15.0 35 B TYR CG 682 174.9 114.3 15.5 38 B TYR CD1 682 173.5 114.0 15.9 39 B TYR CE1 682 173.1 112.7 16.2 38 B TYR CD2 682 175.8 113.2 15.4 39 B TYR CE2 682 175.3 111.9 15.7 39 B TYR CZ 682 174.0 111.7 16.1 39 B TYR OH 682 173.6 110.4 16.3 40 B TYR C 682 177.3 117.0 14.8 33 B TYR O 682 178.2 116.6 14.1 33 B SER N 683 177.1 118.3 14.8 33 B SER CA 683 177.8 119.3 14.0 33 B SER CB 683 177.1 120.7 13.9 34 B SER OG 683 177.6 121.5 15.0 36 B SER C 683 179.3 119.4 14.3 32 B SER O 683 180.1 119.7 13.4 33 B LEU N 684 179.7 119.1 15.5 31 B LEU CA 684 181.0 119.2 16.0 29 B LEU CB 684 181.1 119.8 17.4 28 B LEU CG 684 180.2 121.0 17.7 26 B LEU CD1 684 180.3 121.4 19.1 26 B LEU CD2 684 180.5 122.1 16.8 26 B LEU C 684 181.8 117.9 15.9 30 B LEU O 684 183.0 117.9 15.9 31 B LYS N 685 181.1 116.8 15.9 31 B LYS CA 685 181.6 115.5 15.9 29 B LYS CB 685 180.5 114.4 15.8 29 B LYS CG 685 180.9 113.0 16.0 29 B LYS CD 685 181.6 112.8 17.3 29 B LYS CE 685 181.5 111.4 17.8 30 B LYS NZ 685 182.0 110.4 16.9 32 B LYS C 685 182.6 115.2 14.8 29 B LYS O 685 182.4 115.5 13.6 29 B GLN N 686 183.8 114.7 15.2 30 B GLN CA 686 184.9 114.4 14.3 31 B GLN CB 686 186.2 114.8 14.9 31 B GLN CG 686 186.3 116.2 15.1 31 B GLN CD 686 186.1 116.9 13.8 32 B GLN OE1 686 187.1 117.0 13.0 33 B GLN NE2 686 184.9 117.4 13.5 33 B GLN C 686 185.0 112.9 14.0 32 B GLN O 686 184.7 112.0 14.8 33 B PRO N 687 185.5 112.6 12.7 32 B PRO CD 687 185.8 113.5 11.6 32 B PRO CA 687 185.6 111.2 12.3 31 B PRO CB 687 186.3 111.3 11.0 32 B PRO CG 687 185.7 112.6 10.4 32 B PRO C 687 186.5 110.4 13.3 31 B PRO O 687 186.2 109.2 13.5 33 B ASP N 688 187.5 111.0 13.9 28 B ASP CA 688 188.3 110.3 14.9 26 B ASP CB 688 189.8 110.8 14.9 28 B ASP CG 688 189.9 112.1 15.6 31 B ASP OD1 688 188.9 112.8 15.9 31 B ASP OD2 688 191.1 112.5 15.8 32 B ASP C 688 187.8 110.1 16.3 25 B ASP O 688 188.5 109.6 17.1 26 B GLY N 689 186.6 110.6 16.5 24 B GLY CA 689 185.9 110.4 17.8 24 B GLY C 689 185.9 111.7 18.6 24 B GLY O 689 185.1 111.7 19.6 25 B SER N 690 186.7 112.7 18.3 23 B SER CA 690 186.7 113.9 19.1 24 B SER CB 690 188.1 114.6 18.9 23 B SER OG 690 188.3 115.0 17.6 21 B SER C 690 185.6 114.8 18.5 26 B SER O 690 185.1 114.5 17.4 28 B PHE N 691 185.4 115.9 19.2 25 B PHE CA 691 184.4 117.0 18.8 24 B PHE CB 691 183.3 117.2 19.8 23 B PHE CG 691 182.4 116.0 20.0 22 B PHE CD1 691 182.8 114.9 20.8 21 B PHE CD2 691 181.1 116.0 19.5 20 B PHE CE1 691 182.0 113.8 21.1 20 B PHE CE2 691 180.3 114.9 19.7 21 B PHE CZ 691 180.7 113.9 20.5 21 B PHE C 691 185.2 118.3 18.7 24 B PHE O 691 186.2 118.4 19.4 26 B LEU N 692 184.6 119.2 18.0 25 B LEU CA 692 185.3 120.6 17.9 25 B LEU CB 692 184.9 121.3 16.7 25 B LEU CG 692 185.1 120.7 15.3 25 B LEU CD1 692 184.4 121.5 14.2 24 B LEU CD2 692 186.6 120.5 15.0 25 B LEU C 692 184.6 121.3 19.1 26 B LEU O 692 183.5 120.8 19.6 28 B MET N 693 185.2 122.4 19.6 24 B MET CA 693 184.5 123.1 20.7 23 B MET CB 693 185.5 123.9 21.5 22 B MET CG 693 186.5 123.1 22.4 21 B MET SD 693 185.7 122.3 23.7 23 B MET CE 693 185.1 123.7 24.7 21 B MET C 693 183.4 123.9 20.1 22 B MET O 693 182.4 124.2 20.8 23 B HIS N 694 183.6 124.4 18.9 20 B HIS CA 694 182.6 125.2 18.2 22 B HIS CB 694 182.6 126.6 18.7 21 B HIS CG 694 183.8 127.4 18.5 21 B HIS CD2 694 185.1 127.3 19.1 20 B HIS ND1 694 184.0 128.4 17.6 21 B HIS CE1 694 185.2 128.9 17.6 21 B HIS NE2 694 185.9 128.3 18.5 21 B HIS C 694 182.9 125.0 16.7 24 B HIS O 694 184.0 124.5 16.3 25 B VAL N 695 182.0 125.4 15.9 26 B VAL CA 695 182.2 125.4 14.4 27 B VAL CB 695 180.9 125.8 13.7 27 B VAL CG1 695 181.2 125.9 12.2 26 B VAL CG2 695 179.8 124.9 13.9 26 B VAL C 695 183.4 126.2 14.0 27 B VAL O 695 183.5 127.4 14.3 30 B GLY N 696 184.4 125.5 13.4 27 B GLY CA 696 185.6 126.2 13.1 27 B GLY C 696 186.5 126.4 14.2 27 B GLY O 696 187.5 127.1 14.1 28 B GLY N 697 186.2 125.7 15.4 25 B GLY CA 697 187.0 125.9 16.6 23 B GLY C 697 188.0 124.7 16.8 23 B GLY O 697 187.9 123.7 16.1 25 B GLU N 698 188.8 124.8 17.9 20 B GLU CA 698 189.7 123.8 18.3 18 B GLU CB 698 190.7 124.4 19.3 18 B GLU CG 698 190.1 124.6 20.7 17 B GLU CD 698 189.3 125.9 20.9 18 B GLU OE1 698 189.0 126.6 19.9 17 B GLU OE2 698 189.0 126.2 22.1 18 B GLU C 698 189.2 122.5 18.8 18 B GLU O 698 188.0 122.4 19.2 19 B VAL N 699 190.1 121.5 18.9 18 B VAL CA 699 189.7 120.2 19.4 18 B VAL CB 699 189.9 119.1 18.4 18 B VAL CG1 699 189.8 117.7 19.0 18 B VAL CG2 699 188.8 119.3 17.3 17 B VAL C 699 190.7 119.8 20.6 19 B VAL O 699 191.9 120.0 20.5 20 B ASP N 700 190.1 119.3 21.7 20 B ASP CA 700 190.9 118.9 22.9 20 B ASP CB 700 191.6 120.0 23.6 19 B ASP CG 700 190.7 121.1 24.1 20 B ASP OD1 700 190.0 120.8 25.0 19 B ASP OD2 700 190.8 122.2 23.6 20 B ASP C 700 189.8 118.2 23.7 21 B ASP O 700 188.7 118.4 23.5 23 B VAL N 701 190.3 117.4 24.8 22 B VAL CA 701 189.3 116.7 25.6 22 B VAL CB 701 189.9 115.9 26.8 21 B VAL CG1 701 189.2 114.6 27.0 21 B VAL CG2 701 191.4 115.7 26.6 23 B VAL C 701 188.1 117.4 26.2 23 B VAL O 701 187.1 116.8 26.5 23 B ARG N 702 188.2 118.7 26.4 23 B ARG CA 702 187.1 119.5 27.0 23 B ARG CB 702 187.3 121.0 27.0 22 B ARG CG 702 188.5 121.5 27.9 19 B ARG CD 702 188.7 123.0 27.6 19 B ARG NE 702 189.1 123.3 26.2 19 B ARG CZ 702 188.7 124.4 25.5 20 B ARG NH1 702 189.2 124.5 24.3 20 B ARG NH2 702 188.0 125.3 26.0 20 B ARG C 702 185.8 119.2 26.1 24 B ARG O 702 184.7 119.2 26.7 25 B SER N 703 186.0 119.2 24.8 24 B SER CA 703 184.8 119.0 24.0 25 B SER CB 703 185.2 119.0 22.5 25 B SER OG 703 185.9 117.8 22.2 25 B SER C 703 184.1 117.7 24.2 26 B SER O 703 182.9 117.6 24.2 28 B ALA N 704 184.9 116.6 24.6 26 B ALA CA 704 184.4 115.3 24.8 27 B ALA CB 704 185.5 114.3 24.9 27 B ALA C 704 183.5 115.3 26.1 28 B ALA O 704 182.4 114.7 26.1 26 B TYR N 705 184.0 115.9 27.2 28 B TYR CA 705 183.4 116.0 28.5 29 B TYR CB 705 184.3 116.5 29.6 29 B TYR CG 705 183.7 116.9 30.9 32 B TYR CD1 705 183.1 116.0 31.7 32 B TYR CE1 705 182.5 116.3 32.9 33 B TYR CD2 705 183.7 118.2 31.3 32 B TYR CE2 705 183.1 118.6 32.5 32 B TYR CZ 705 182.5 117.7 33.3 33 B TYR OH 705 181.9 118.0 34.5 34 B TYR C 705 182.1 116.9 28.4 29 B TYR O 705 181.0 116.6 28.9 29 B CYS N 706 182.3 118.0 27.7 27 B CYS CA 706 181.2 119.0 27.6 25 B CYS CB 706 181.6 120.2 26.8 25 B CYS SG 706 182.7 121.2 27.7 25 B CYS C 706 180.0 118.3 26.8 27 B CYS O 706 178.9 118.4 27.3 29 B ALA N 707 180.3 117.6 25.7 27 B ALA CA 707 179.3 116.9 25.0 26 B ALA CB 707 179.8 116.4 23.7 25 B ALA C 707 178.6 115.8 25.8 28 B ALA O 707 177.4 115.8 26.0 29 B ALA N 708 179.5 115.0 26.4 28 B ALA CA 708 179.0 113.9 27.2 29 B ALA CB 708 180.1 113.0 27.7 28 B ALA C 708 178.1 114.3 28.4 30 B ALA O 708 177.1 113.7 28.7 32 B SER N 709 178.5 115.4 29.1 31 B SER CA 709 177.8 115.9 30.2 30 B SER CB 709 178.6 117.0 30.9 30 B SER OG 709 177.9 117.7 31.9 30 B SER C 709 176.4 116.5 29.9 30 B SER O 709 175.4 116.2 30.5 30 B VAL N 710 176.3 117.3 28.8 31 B VAL CA 710 175.0 117.9 28.4 32 B VAL CB 710 175.2 119.1 27.4 33 B VAL CG1 710 175.9 120.2 28.1 33 B VAL CG2 710 175.9 118.6 26.1 33 B VAL C 710 174.1 116.9 27.7 34 B VAL O 710 172.9 116.9 27.9 35 B ALA N 711 174.7 116.0 26.9 35 B ALA CA 711 173.9 115.0 26.1 34 B ALA CB 711 174.7 114.3 25.1 34 B ALA C 711 173.3 114.0 27.1 35 B ALA O 711 172.1 113.6 26.9 36 B SER N 712 174.1 113.5 28.1 36 B SER CA 712 173.5 112.5 29.0 36 B SER CB 712 174.7 112.0 29.9 36 B SER OG 712 175.4 113.0 30.5 37 B SER C 712 172.4 113.1 29.9 37 B SER O 712 171.3 112.6 30.0 38 B LEU N 713 172.7 114.3 30.6 36 B LEU CA 713 171.7 114.9 31.4 35 B LEU CB 713 172.3 116.3 32.0 33 B LEU CG 713 173.4 116.2 33.0 33 B LEU CD1 713 173.9 117.6 33.3 32 B LEU CD2 713 172.9 115.5 34.3 32 B LEU C 713 170.4 115.2 30.7 35 B LEU O 713 169.4 114.8 31.2 36 B THR N 714 170.5 115.7 29.5 36 B THR CA 714 169.3 116.0 28.7 37 B THR CB 714 169.4 117.2 27.7 36 B THR OG1 714 170.3 116.8 26.6 37 B THR CG2 714 170.0 118.4 28.4 36 B THR C 714 168.8 114.8 27.9 38 B THR O 714 167.8 114.9 27.2 39 B ASN N 715 169.4 113.6 28.1 39 B ASN CA 715 169.0 112.4 27.4 38 B ASN CB 715 167.6 112.0 28.0 40 B ASN CG 715 167.0 110.8 27.3 41 B ASN OD1 715 167.7 109.9 26.9 42 B ASN ND2 715 165.7 110.9 27.1 41 B ASN C 715 168.8 112.6 25.9 39 B ASN O 715 167.7 112.5 25.3 40 B ILE N 716 169.9 112.8 25.2 36 B ILE CA 716 169.9 113.0 23.7 34 B ILE CB 716 170.2 114.4 23.3 35 B ILE CG2 716 169.0 115.3 23.4 35 B ILE CG1 716 171.4 114.9 24.0 35 B ILE CD1 716 172.0 116.1 23.4 36 B ILE C 716 170.9 112.0 23.2 33 B ILE O 716 171.2 112.1 22.0 31 B ILE N 717 171.5 111.2 24.0 32 B ILE CA 717 172.5 110.2 23.5 34 B ILE CB 717 173.3 109.6 24.7 33 B ILE CG2 717 174.5 108.8 24.0 31 B ILE CG1 717 173.9 110.6 25.6 32 B ILE CD1 717 174.8 110.0 26.6 31 B ILE C 717 171.9 109.1 22.6 36 B ILE O 717 171.2 108.2 23.1 37 B THR N 718 172.2 109.3 21.3 38 B THR CA 718 171.8 108.3 20.4 41 B THR CB 718 171.8 108.9 19.0 41 B THR OG1 718 173.2 109.2 18.6 42 B THR CG2 718 171.0 110.2 18.9 41 B THR C 718 172.8 107.2 20.4 42 B THR O 718 173.8 107.2 21.2 43 B PRO N 719 172.6 106.1 19.6 44 B PRO CD 719 171.5 105.8 18.7 44 B PRO CA 719 173.6 105.0 19.6 43 B PRO CB 719 172.9 103.9 18.8 44 B PRO CG 719 172.1 104.8 17.8 45 B PRO C 719 175.0 105.3 19.0 43 B PRO O 719 176.0 104.8 19.4 43 B ASP N 720 175.0 106.2 18.0 40 B ASP CA 720 176.3 106.5 17.4 40 B ASP CB 720 176.1 106.4 15.8 41 B ASP CG 720 175.3 107.4 15.2 43 B ASP OD1 720 175.5 107.8 14.1 45 B ASP OD2 720 174.3 107.8 15.9 44 B ASP C 720 176.8 107.9 17.7 39 B ASP O 720 177.8 108.4 17.0 38 B LEU N 721 176.2 108.6 18.6 37 B LEU CA 721 176.7 110.0 19.0 35 B LEU CB 721 175.8 110.5 20.1 34 B LEU CG 721 176.3 111.9 20.6 33 B LEU CD1 721 176.4 112.9 19.5 32 B LEU CD2 721 175.4 112.4 21.7 33 B LEU C 721 178.2 110.0 19.4 35 B LEU O 721 178.9 110.7 18.7 35 B PHE N 722 178.5 109.2 20.4 34 B PHE CA 722 179.9 109.2 20.9 36 B PHE CB 722 179.8 109.1 22.4 36 B PHE CG 722 179.2 110.3 23.1 36 B PHE CD1 722 178.0 110.3 23.7 35 B PHE CD2 722 179.9 111.5 23.0 35 B PHE CE1 722 177.4 111.4 24.3 34 B PHE CE2 722 179.4 112.7 23.6 34 B PHE CZ 722 178.1 112.6 24.2 34 B PHE C 722 180.7 108.0 20.3 37 B PHE O 722 181.6 107.5 21.0 37 B GLU N 723 180.4 107.7 19.1 40 B GLU CA 723 181.1 106.6 18.4 41 B GLU CB 723 180.6 106.4 17.0 45 B GLU CG 723 180.9 105.1 16.3 50 B GLU CD 723 179.9 104.0 16.7 54 B GLU OE1 723 179.0 103.7 15.9 56 B GLU OE2 723 180.0 103.5 17.8 57 B GLU C 723 182.6 106.9 18.3 39 B GLU O 723 183.0 107.8 17.6 38 B GLY N 724 183.4 106.0 18.9 37 B GLY CA 724 184.9 106.2 18.8 35 B GLY C 724 185.4 107.3 19.8 34 B GLY O 724 186.6 107.5 19.8 35 B THR N 725 184.5 107.9 20.6 34 B THR CA 725 184.9 108.9 21.5 33 B THR CB 725 183.7 109.7 22.1 34 B THR OG1 725 183.0 110.3 21.0 30 B THR CG2 725 184.2 110.8 23.0 30 B THR C 725 185.7 108.4 22.7 32 B THR O 725 186.7 109.0 23.1 33 B ALA N 726 185.4 107.2 23.2 30 B ALA CA 726 186.1 106.6 24.3 30 B ALA CB 726 185.4 105.4 24.9 30 B ALA C 726 187.5 106.3 23.9 31 B ALA O 726 188.5 106.3 24.7 32 B GLU N 727 187.7 105.9 22.6 30 B GLU CA 727 189.0 105.5 22.1 30 B GLU CB 727 188.8 104.7 20.8 32 B GLU CG 727 188.4 103.3 21.0 34 B GLU CD 727 186.9 103.1 21.3 36 B GLU OE1 727 186.5 102.0 21.8 38 B GLU OE2 727 186.1 104.0 20.9 36 B GLU C 727 189.9 106.7 21.9 29 B GLU O 727 191.1 106.6 22.1 30 B TRP N 728 189.4 107.8 21.5 28 B TRP CA 728 190.2 109.0 21.3 27 B TRP CB 728 189.3 110.1 20.7 25 B TRP CG 728 190.1 111.3 20.2 24 B TRP CD2 728 190.4 112.4 21.0 25 B TRP CE2 728 191.2 113.2 20.2 25 B TRP CE3 728 190.0 112.9 22.3 25 B TRP CD1 728 190.8 111.4 19.1 24 B TRP NE1 728 191.4 112.6 19.0 25 B TRP CZ2 728 191.7 114.5 20.6 24 B TRP CZ3 728 190.5 114.1 22.7 23 B TRP CH2 728 191.3 114.9 21.8 23 B TRP C 728 190.6 109.5 22.7 27 B TRP O 728 191.8 109.8 23.0 28 B ILE N 729 189.7 109.6 23.7 26 B ILE CA 729 190.0 110.0 25.0 24 B ILE CB 729 188.8 110.0 25.9 22 B ILE CG2 729 189.1 110.3 27.3 22 B ILE CG1 729 187.7 111.0 25.4 23 B ILE CD1 729 186.4 111.0 26.2 24 B ILE C 729 191.1 109.1 25.7 25 B ILE O 729 191.9 109.6 26.4 27 B ALA N 730 191.1 107.8 25.3 26 B ALA CA 730 192.1 106.9 25.9 26 B ALA CB 730 191.6 105.4 25.7 26 B ALA C 730 193.4 107.1 25.2 25 B ALA O 730 194.5 106.7 25.7 26 B ARG N 731 193.4 107.8 24.0 25 B ARG CA 731 194.7 108.1 23.4 24 B ARG CB 731 194.4 108.4 21.9 25 B ARG CG 731 194.0 107.1 21.1 25 B ARG CD 731 194.6 107.2 19.7 25 B ARG NE 731 193.9 108.1 18.9 28 B ARG CZ 731 194.4 109.1 18.1 28 B ARG NH1 731 195.7 109.3 18.2 26 B ARG NH2 731 193.6 109.8 17.3 28 B ARG C 731 195.3 109.3 24.0 25 B ARG O 731 196.5 109.6 23.8 27 B CYS N 732 194.5 110.1 24.8 23 B CYS CA 732 195.0 111.3 25.5 22 B CYS CB 732 193.9 112.2 25.8 22 B CYS SG 732 193.0 112.8 24.3 23 B CYS C 732 195.8 110.9 26.7 23 B CYS O 732 196.6 111.6 27.2 23 B GLN N 733 195.7 109.6 27.2 23 B GLN CA 733 196.4 109.1 28.3 24 B GLN CB 733 195.8 107.8 28.9 24 B GLN CG 733 196.6 107.3 30.1 25 B GLN CD 733 195.9 106.2 30.9 26 B GLN OE1 733 195.5 105.2 30.3 27 B GLN NE2 733 195.8 106.4 32.2 24 B GLN C 733 197.9 108.8 27.9 25 B GLN O 733 198.1 108.0 27.0 26 B ASN N 734 198.9 109.5 28.5 26 B ASN CA 734 200.3 109.3 28.2 25 B ASN CB 734 200.9 110.7 27.9 25 B ASN CG 734 201.2 111.4 29.2 25 B ASN OD1 734 200.7 111.0 30.2 24 B ASN ND2 734 202.0 112.5 29.1 26 B ASN C 734 201.1 108.5 29.1 25 B ASN O 734 200.6 108.0 30.1 26 B TRP N 735 202.4 108.5 28.9 24 B TRP CA 735 203.4 107.8 29.8 24 B TRP CB 735 204.8 108.0 29.3 23 B TRP CG 735 205.2 109.5 29.2 22 B TRP CD2 735 205.9 110.3 30.1 20 B TRP CE2 735 206.0 111.6 29.6 20 B TRP CE3 735 206.6 110.0 31.3 20 B TRP CD1 735 204.8 110.4 28.2 22 B TRP NE1 735 205.3 111.6 28.5 21 B TRP CZ2 735 206.6 112.6 30.3 19 B TRP CZ3 735 207.2 111.0 32.0 20 B TRP CH2 735 207.2 112.3 31.5 20 B TRP C 735 203.4 108.1 31.3 27 B TRP O 735 203.9 107.4 32.1 28 B GLU N 736 202.7 109.2 31.7 27 B GLU CA 736 202.7 109.7 33.1 26 B GLU CB 736 202.5 111.2 33.1 26 B GLU CG 736 203.5 112.0 32.3 27 B GLU CD 736 203.2 113.5 32.4 27 B GLU OE1 736 202.8 114.1 31.3 27 B GLU OE2 736 203.3 114.2 33.4 28 B GLU C 736 201.5 109.0 33.8 25 B GLU O 736 201.4 109.2 35.1 27 B GLY N 737 200.5 108.4 33.1 23 B GLY CA 737 199.4 107.8 33.8 20 B GLY C 737 198.3 108.8 33.7 20 B GLY O 737 197.1 108.4 33.8 21 B GLY N 738 198.6 110.1 33.4 21 B GLY CA 738 197.5 111.1 33.3 20 B GLY C 738 197.1 111.3 31.9 20 B GLY O 738 197.6 110.7 30.9 21 B ILE N 739 196.1 112.2 31.7 19 B ILE CA 739 195.5 112.5 30.4 19 B ILE CB 739 194.0 112.3 30.5 17 B ILE CG2 739 193.3 112.6 29.2 18 B ILE CG1 739 193.7 110.9 31.0 15 B ILE CD1 739 192.3 110.5 30.9 14 B ILE C 739 195.9 113.9 29.9 20 B ILE O 739 196.0 114.8 30.7 24 B GLY N 740 196.2 114.1 28.6 20 B GLY CA 740 196.6 115.4 28.1 17 B GLY C 740 195.4 116.0 27.3 17 B GLY O 740 194.4 115.4 27.1 17 B GLY N 741 195.6 117.2 26.7 18 B GLY CA 741 194.6 117.9 26.0 18 B GLY C 741 194.2 117.1 24.7 19 B GLY O 741 193.0 117.1 24.3 19 B VAL N 742 195.2 116.6 24.0 21 B VAL CA 742 195.0 115.8 22.8 21 B VAL CB 742 195.3 116.7 21.5 20 B VAL CG1 742 194.2 117.7 21.3 19 B VAL CG2 742 196.7 117.4 21.6 19 B VAL C 742 196.1 114.7 22.8 21 B VAL O 742 197.0 114.8 23.6 23 B PRO N 743 195.9 113.6 22.1 20 B PRO CD 743 194.8 113.2 21.2 18 B PRO CA 743 196.9 112.5 22.2 20 B PRO CB 743 196.5 111.6 21.0 19 B PRO CG 743 195.1 111.7 21.0 19 B PRO C 743 198.4 113.1 21.9 21 B PRO O 743 198.6 113.9 21.0 21 B GLY N 744 199.3 112.7 22.8 22 B GLY CA 744 200.7 113.2 22.7 22 B GLY C 744 201.1 114.3 23.7 24 B GLY O 744 202.2 114.5 23.9 23 B MET N 745 200.0 114.9 24.2 23 B MET CA 745 200.3 116.0 25.2 24 B MET CB 745 199.3 117.1 25.0 25 B MET CG 745 199.6 118.0 23.9 27 B MET SD 745 200.8 119.3 24.3 30 B MET CE 745 202.2 118.5 24.9 28 B MET C 745 200.5 115.6 26.6 24 B MET O 745 200.1 114.5 27.1 25 B GLU N 746 201.2 116.5 27.4 24 B GLU CA 746 201.5 116.4 28.8 23 B GLU CB 746 202.3 117.6 29.3 24 B GLU CG 746 202.8 117.5 30.7 26 B GLU CD 746 203.4 118.8 31.1 28 B GLU OE1 746 203.2 119.9 30.4 29 B GLU OE2 746 204.0 118.9 32.2 30 B GLU C 746 200.2 116.2 29.6 21 B GLU O 746 199.2 116.8 29.4 22 B ALA N 747 200.3 115.3 30.6 21 B ALA CA 747 199.2 115.0 31.5 19 B ALA CB 747 199.5 113.9 32.4 19 B ALA C 747 198.9 116.3 32.2 18 B ALA O 747 199.8 116.9 32.8 17 B HIS N 748 197.6 116.6 32.2 18 B HIS CA 748 197.2 117.9 32.9 19 B HIS CB 748 196.8 118.8 31.7 18 B HIS CG 748 196.5 120.2 32.2 19 B HIS CD2 748 197.3 121.3 32.3 19 B HIS ND1 748 195.3 120.5 32.7 21 B HIS CE1 748 195.3 121.8 33.0 21 B HIS NE2 748 196.5 122.3 32.8 21 B HIS C 748 195.9 117.6 33.7 20 B HIS O 748 195.1 116.8 33.2 23 B GLY N 749 195.8 118.2 34.8 21 B GLY CA 749 194.7 118.0 35.7 20 B GLY C 749 193.3 118.3 35.2 21 B GLY O 749 192.3 117.7 35.5 22 B GLY N 750 193.2 119.5 34.5 21 B GLY CA 750 191.8 119.9 34.0 20 B GLY C 750 191.4 119.0 32.9 22 B GLY O 750 190.2 118.8 32.7 24 B TYR N 751 192.4 118.4 32.1 23 B TYR CA 751 192.1 117.6 31.0 21 B TYR CB 751 193.2 117.6 29.9 21 B TYR CG 751 193.3 118.9 29.2 22 B TYR CD1 751 194.5 119.6 29.0 21 B TYR CE1 751 194.5 120.8 28.3 21 B TYR CD2 751 192.1 119.4 28.6 22 B TYR CE2 751 192.2 120.6 27.8 21 B TYR CZ 751 193.4 121.3 27.7 22 B TYR OH 751 193.4 122.4 26.9 23 B TYR C 751 191.8 116.1 31.4 21 B TYR O 751 191.1 115.4 30.8 22 B THR N 752 192.5 115.7 32.5 20 B THR CA 752 192.4 114.4 33.1 21 B THR CB 752 193.4 114.1 34.1 21 B THR OG1 752 194.7 114.2 33.6 20 B THR CG2 752 193.3 112.7 34.6 20 B THR C 752 191.0 114.3 33.7 23 B THR O 752 190.4 113.2 33.6 27 B PHE N 753 190.5 115.4 34.3 24 B PHE CA 753 189.1 115.3 34.8 23 B PHE CB 753 188.8 116.6 35.6 22 B PHE CG 753 187.3 116.7 36.0 22 B PHE CD1 753 186.8 116.0 37.1 23 B PHE CD2 753 186.5 117.4 35.2 23 B PHE CE1 753 185.5 116.0 37.4 23 B PHE CE2 753 185.1 117.4 35.4 24 B PHE CZ 753 184.6 116.7 36.5 23 B PHE C 753 188.2 115.2 33.6 24 B PHE O 753 187.2 114.4 33.7 28 B CYS N 754 188.4 116.0 32.6 24 B CYS CA 754 187.5 115.9 31.4 24 B CYS CB 754 187.9 116.9 30.3 23 B CYS SG 754 187.5 118.6 30.8 19 B CYS C 754 187.5 114.5 30.8 25 B CYS O 754 186.4 114.0 30.5 25 B GLY N 755 188.6 113.9 30.7 25 B GLY CA 755 188.7 112.5 30.1 25 B GLY C 755 188.1 111.5 31.0 26 B GLY O 755 187.2 110.8 30.5 26 B LEU N 756 188.5 111.4 32.3 26 B LEU CA 756 188.0 110.4 33.2 26 B LEU CB 756 188.7 110.5 34.5 26 B LEU CG 756 188.2 109.4 35.5 28 B LEU CD1 756 188.4 108.0 34.9 29 B LEU CD2 756 189.0 109.5 36.8 27 B LEU C 756 186.5 110.6 33.3 27 B LEU O 756 185.7 109.7 33.0 29 B ALA N 757 186.0 111.8 33.7 26 B ALA CA 757 184.6 112.0 33.8 26 B ALA CB 757 184.3 113.4 34.2 25 B ALA C 757 183.8 111.7 32.6 27 B ALA O 757 182.6 111.2 32.6 28 B ALA N 758 184.4 112.0 31.4 27 B ALA CA 758 183.7 111.7 30.1 27 B ALA CB 758 184.5 112.3 29.0 26 B ALA C 758 183.6 110.2 30.0 28 B ALA O 758 182.6 109.7 29.5 30 B LEU N 759 184.6 109.4 30.4 29 B LEU CA 759 184.6 108.0 30.3 29 B LEU CB 759 186.0 107.4 30.4 28 B LEU CG 759 186.9 107.6 29.2 28 B LEU CD1 759 188.3 107.0 29.4 27 B LEU CD2 759 186.3 106.9 28.0 27 B LEU C 759 183.6 107.4 31.3 30 B LEU O 759 183.0 106.4 31.0 30 B VAL N 760 183.5 108.0 32.5 30 B VAL CA 760 182.6 107.5 33.5 29 B VAL CB 760 182.7 108.3 34.8 29 B VAL CG1 760 181.5 108.0 35.7 27 B VAL CG2 760 184.0 108.1 35.4 29 B VAL C 760 181.1 107.6 32.9 31 B VAL O 760 180.3 106.7 33.0 32 B ILE N 761 180.9 108.8 32.3 32 B ILE CA 761 179.5 109.0 31.7 33 B ILE CB 761 179.5 110.4 31.1 33 B ILE CG2 761 178.1 110.6 30.4 33 B ILE CG1 761 179.7 111.5 32.1 32 B ILE CD1 761 179.6 112.9 31.6 32 B ILE C 761 179.3 107.9 30.6 35 B ILE O 761 178.2 107.2 30.7 35 B LEU N 762 180.2 107.7 29.7 36 B LEU CA 762 180.1 106.7 28.6 36 B LEU CB 762 181.2 107.0 27.6 33 B LEU CG 762 181.1 108.3 26.8 30 B LEU CD1 762 182.2 108.3 25.7 29 B LEU CD2 762 179.7 108.4 26.1 29 B LEU C 762 180.2 105.3 29.2 39 B LEU O 762 180.0 104.3 28.4 39 B LYS N 763 180.5 105.2 30.5 43 B LYS CA 763 180.6 103.9 31.1 45 B LYS CB 763 179.2 103.2 31.0 47 B LYS CG 763 178.1 104.1 31.4 51 B LYS CD 763 176.7 103.4 31.1 55 B LYS CE 763 175.8 103.6 32.3 57 B LYS NZ 763 174.6 102.7 32.3 59 B LYS C 763 181.7 103.1 30.6 45 B LYS O 763 181.6 101.9 30.4 46 B LYS N 764 182.8 103.8 30.3 46 B LYS CA 764 184.0 103.2 29.8 46 B LYS CB 764 184.1 103.6 28.3 46 B LYS CG 764 183.0 103.0 27.5 48 B LYS CD 764 183.2 103.3 26.0 48 B LYS CE 764 182.1 102.5 25.2 50 B LYS NZ 764 182.1 101.1 25.5 50 B LYS C 764 185.3 103.6 30.5 46 B LYS O 764 186.4 103.6 29.8 47 B GLU N 765 185.3 103.9 31.7 47 B GLU CA 765 186.5 104.2 32.5 47 B GLU CB 765 186.2 104.2 34.0 48 B GLU CG 765 184.9 104.8 34.4 51 B GLU CD 765 183.8 103.7 34.4 53 B GLU OE1 765 183.1 103.6 33.4 53 B GLU OE2 765 183.5 103.1 35.5 54 B GLU C 765 187.6 103.2 32.2 48 B GLU O 765 188.8 103.6 32.1 49 B ARG N 766 187.2 102.0 32.1 49 B ARG CA 766 188.1 100.9 31.8 49 B ARG CB 766 187.3 99.6 31.9 52 B ARG CG 766 187.3 98.9 33.3 56 B ARG CD 766 186.0 98.3 33.7 59 B ARG NE 766 185.1 99.3 34.4 62 B ARG CZ 766 185.3 99.7 35.6 62 B ARG NH1 766 184.5 100.7 36.1 62 B ARG NH2 766 186.2 99.2 36.4 63 B ARG C 766 188.9 101.0 30.5 47 B ARG O 766 189.8 100.1 30.3 47 B SER N 767 188.7 102.0 29.7 43 B SER CA 767 189.4 102.1 28.4 42 B SER CB 767 188.8 103.1 27.5 42 B SER OG 767 187.6 102.5 26.9 43 B SER C 767 190.8 102.7 28.8 41 B SER O 767 191.6 103.0 27.9 43 B LEU N 768 191.0 103.0 30.1 40 B LEU CA 768 192.3 103.6 30.6 39 B LEU CB 768 192.0 104.8 31.3 40 B LEU CG 768 191.3 106.0 30.6 41 B LEU CD1 768 191.0 107.1 31.6 41 B LEU CD2 768 192.1 106.4 29.5 42 B LEU C 768 193.0 102.6 31.5 39 B LEU O 768 192.5 101.6 31.9 40 B ASN N 769 194.3 103.0 31.8 36 B ASN CA 769 195.0 102.2 32.8 34 B ASN CB 769 196.5 102.1 32.5 33 B ASN CG 769 197.3 101.5 33.5 32 B ASN OD1 769 196.8 101.3 34.7 33 B ASN ND2 769 198.5 101.1 33.2 33 B ASN C 769 194.8 102.9 34.1 34 B ASN O 769 195.4 103.9 34.3 35 B LEU N 770 193.8 102.5 34.8 35 B LEU CA 770 193.4 103.1 36.1 33 B LEU CB 770 192.0 102.6 36.6 31 B LEU CG 770 190.9 102.7 35.5 31 B LEU CD1 770 189.6 102.0 36.0 30 B LEU CD2 770 190.6 104.2 35.3 30 B LEU C 770 194.4 103.0 37.2 35 B LEU O 770 194.4 103.7 38.1 36 B LYS N 771 195.3 102.1 37.0 37 B LYS CA 771 196.3 101.9 38.0 40 B LYS CB 771 197.1 100.6 37.8 43 B LYS CG 771 196.4 99.4 38.4 46 B LYS CD 771 196.5 99.3 39.9 50 B LYS CE 771 195.6 100.3 40.7 51 B LYS NZ 771 194.2 99.9 40.7 52 B LYS C 771 197.2 103.1 38.0 41 B LYS O 771 197.2 104.0 38.8 43 B SER N 772 197.9 103.3 36.8 42 B SER CA 772 198.8 104.4 36.6 40 B SER CB 772 199.6 104.3 35.3 40 B SER OG 772 198.6 104.3 34.2 40 B SER C 772 198.1 105.8 36.7 39 B SER O 772 198.7 106.7 37.2 40 B LEU N 773 196.9 105.8 36.3 37 B LEU CA 773 196.1 107.1 36.4 36 B LEU CB 773 194.8 107.0 35.8 33 B LEU CG 773 193.7 108.1 36.1 31 B LEU CD1 773 194.3 109.4 35.9 32 B LEU CD2 773 192.6 107.9 35.1 32 B LEU C 773 196.1 107.4 37.9 38 B LEU O 773 196.3 108.6 38.3 40 B LEU N 774 195.8 106.4 38.7 37 B LEU CA 774 195.7 106.6 40.2 37 B LEU CB 774 195.2 105.3 40.9 37 B LEU CG 774 195.0 105.4 42.4 36 B LEU CD1 774 193.9 106.5 42.7 35 B LEU CD2 774 194.5 104.1 42.9 36 B LEU C 774 197.0 107.1 40.8 37 B LEU O 774 197.0 108.0 41.6 39 B GLN N 775 198.1 106.5 40.4 37 B GLN CA 775 199.4 106.9 40.9 38 B GLN CB 775 200.5 105.9 40.4 40 B GLN CG 775 201.9 106.4 39.9 45 B GLN CD 775 202.0 106.6 38.4 48 B GLN OE1 775 202.4 105.6 37.7 49 B GLN NE2 775 201.6 107.7 37.8 50 B GLN C 775 199.8 108.3 40.5 37 B GLN O 775 200.3 109.1 41.3 37 B TRP N 776 199.3 108.7 39.2 33 B TRP CA 776 199.6 110.0 38.7 29 B TRP CB 776 199.2 110.1 37.3 28 B TRP CG 776 199.5 111.5 36.7 27 B TRP CD2 776 198.4 112.5 36.5 26 B TRP CE2 776 199.1 113.7 35.9 26 B TRP CE3 776 197.1 112.6 36.6 25 B TRP CD1 776 200.6 112.1 36.3 27 B TRP NE1 776 200.4 113.4 35.8 26 B TRP CZ2 776 198.4 114.9 35.6 26 B TRP CZ3 776 196.4 113.8 36.3 25 B TRP CH2 776 197.1 114.9 35.8 25 B TRP C 776 198.8 111.1 39.5 27 B TRP O 776 199.4 112.0 40.1 27 B VAL N 777 197.5 110.9 39.6 27 B VAL CA 777 196.7 111.9 40.4 28 B VAL CB 777 195.1 111.5 40.3 27 B VAL CG1 777 194.8 110.3 41.1 27 B VAL CG2 777 194.3 112.7 40.7 26 B VAL C 777 197.1 112.1 41.8 30 B VAL O 777 197.3 113.2 42.3 31 B THR N 778 197.3 111.0 42.5 31 B THR CA 778 197.8 111.0 43.9 31 B THR CB 778 197.8 109.6 44.5 30 B THR OG1 778 198.8 108.8 43.8 29 B THR CG2 778 196.4 109.0 44.5 30 B THR C 778 199.2 111.7 44.0 32 B THR O 778 199.5 112.2 45.1 34 B SER N 779 200.0 111.7 43.0 31 B SER CA 779 201.2 112.3 43.1 29 B SER CB 779 202.1 111.8 42.0 28 B SER OG 779 202.3 110.4 42.1 29 B SER C 779 201.1 113.8 43.0 29 B SER O 779 202.0 114.6 43.3 30 B ARG N 780 199.9 114.3 42.5 28 B ARG CA 780 199.7 115.7 42.3 28 B ARG CB 780 198.5 115.9 41.3 27 B ARG CG 780 198.8 115.2 39.9 24 B ARG CD 780 199.7 116.0 39.0 20 B ARG NE 780 201.1 116.0 39.5 20 B ARG CZ 780 201.9 114.9 39.4 20 B ARG NH1 780 201.5 113.8 38.9 21 B ARG NH2 780 203.1 115.0 39.9 21 B ARG C 780 199.4 116.5 43.5 31 B ARG O 780 199.3 117.7 43.4 32 B GLN N 781 199.2 115.9 44.7 33 B GLN CA 781 198.9 116.6 45.9 33 B GLN CB 781 198.2 115.8 46.9 33 B GLN CG 781 197.8 116.7 48.1 33 B GLN CD 781 196.8 116.0 49.0 32 B GLN OE1 781 196.8 114.8 49.2 35 B GLN NE2 781 195.8 116.8 49.4 31 B GLN C 781 200.3 117.0 46.4 34 B GLN O 781 201.2 116.2 46.5 34 B MET N 782 200.4 118.3 46.8 36 B MET CA 782 201.6 118.9 47.3 38 B MET CB 782 201.6 120.4 47.2 38 B MET CG 782 201.4 120.9 45.8 38 B MET SD 782 202.5 120.2 44.6 37 B MET CE 782 203.9 121.3 44.8 36 B MET C 782 201.8 118.5 48.8 40 B MET O 782 201.1 119.0 49.7 39 B ARG N 783 202.9 117.7 49.0 41 B ARG CA 783 203.2 117.2 50.4 41 B ARG CB 783 204.5 116.4 50.3 40 B ARG CG 783 205.7 117.2 49.9 41 B ARG CD 783 206.8 116.3 49.3 42 B ARG NE 783 207.1 115.2 50.2 44 B ARG CZ 783 207.2 114.0 49.8 46 B ARG NH1 783 207.2 113.6 48.5 45 B ARG NH2 783 207.4 113.0 50.7 47 B ARG C 783 203.3 118.4 51.4 41 B ARG O 783 202.8 118.2 52.5 42 B PHE N 784 203.9 119.5 51.0 41 B PHE CA 784 204.0 120.6 51.9 40 B PHE CB 784 205.3 121.4 51.6 40 B PHE CG 784 205.5 122.5 52.5 40 B PHE CD1 784 206.4 122.4 53.6 41 B PHE CD2 784 204.8 123.7 52.4 41 B PHE CE1 784 206.5 123.4 54.5 41 B PHE CE2 784 204.9 124.7 53.3 40 B PHE CZ 784 205.8 124.5 54.4 41 B PHE C 784 202.8 121.5 51.9 39 B PHE O 784 202.4 122.0 52.9 42 B GLU N 785 202.2 121.8 50.7 37 B GLU CA 785 201.1 122.7 50.7 36 B GLU CB 785 201.0 123.5 49.4 37 B GLU CG 785 202.3 124.2 49.0 37 B GLU CD 785 203.2 123.4 48.1 38 B GLU OE1 785 203.4 123.9 47.0 39 B GLU OE2 785 203.7 122.4 48.6 41 B GLU C 785 199.8 122.1 51.1 35 B GLU O 785 198.9 122.8 51.6 36 B GLY N 786 199.6 120.9 50.6 34 B GLY CA 786 198.3 120.2 50.9 32 B GLY C 786 197.4 120.2 49.7 33 B GLY O 786 196.5 119.3 49.6 34 B GLY N 787 197.4 121.3 48.9 32 B GLY CA 787 196.6 121.4 47.8 31 B GLY C 787 197.2 120.7 46.6 30 B GLY O 787 198.2 120.1 46.7 29 B PHE N 788 196.5 120.7 45.4 29 B PHE CA 788 196.9 120.0 44.2 29 B PHE CB 788 195.8 119.3 43.6 29 B PHE CG 788 195.4 118.0 44.3 30 B PHE CD1 788 194.5 118.0 45.3 29 B PHE CD2 788 196.0 116.8 43.8 30 B PHE CE1 788 194.2 116.8 45.9 29 B PHE CE2 788 195.6 115.6 44.4 30 B PHE CZ 788 194.7 115.6 45.5 30 B PHE C 788 197.6 120.9 43.1 29 B PHE O 788 197.4 122.1 43.0 29 B GLN N 789 198.4 120.2 42.3 29 B GLN CA 789 199.0 120.9 41.2 28 B GLN CB 789 200.5 120.6 41.2 27 B GLN CG 789 201.0 119.2 40.9 24 B GLN CD 789 202.5 119.1 41.1 24 B GLN OE1 789 203.0 118.0 41.0 26 B GLN NE2 789 203.2 120.2 41.4 24 B GLN C 789 198.4 120.3 39.9 27 B GLN O 789 197.8 119.2 40.0 29 B GLY N 790 198.4 121.1 38.8 26 B GLY CA 790 197.7 120.6 37.6 24 B GLY C 790 198.6 119.7 36.8 24 B GLY O 790 198.1 118.9 36.1 23 B ARG N 791 199.9 119.9 36.9 23 B ARG CA 791 200.9 119.2 36.2 24 B ARG CB 791 201.4 120.0 35.0 23 B ARG CG 791 200.5 120.1 33.8 23 B ARG CD 791 201.1 120.8 32.6 24 B ARG NE 791 200.8 122.2 32.6 26 B ARG CZ 791 201.4 123.1 31.9 25 B ARG NH1 791 202.4 122.7 31.0 24 B ARG NH2 791 201.1 124.4 31.9 25 B ARG C 791 202.1 118.9 37.0 23 B ARG O 791 202.5 119.6 37.9 25 B CYS N 792 202.8 117.7 36.8 23 B CYS CA 792 204.0 117.4 37.6 23 B CYS CB 792 204.6 116.1 37.0 22 B CYS SG 792 206.2 115.8 37.9 23 B CYS C 792 205.0 118.5 37.5 23 B CYS O 792 205.2 119.1 36.5 25 B ASN N 793 205.5 118.9 38.7 25 B ASN CA 793 206.5 120.0 38.7 26 B ASN CB 793 207.7 119.7 37.9 26 B ASN CG 793 208.8 119.0 38.6 27 B ASN OD1 793 209.1 119.3 39.8 26 B ASN ND2 793 209.5 118.0 38.0 26 B ASN C 793 206.0 121.4 38.4 26 B ASN O 793 206.7 122.2 37.9 26 B LYS N 794 204.7 121.6 38.7 25 B LYS CA 794 204.1 123.0 38.5 26 B LYS CB 794 202.8 123.0 37.6 26 B LYS CG 794 203.1 122.7 36.2 27 B LYS CD 794 204.0 123.7 35.5 28 B LYS CE 794 203.3 125.0 35.4 30 B LYS NZ 794 202.0 124.9 34.7 31 B LYS C 794 203.8 123.4 39.9 27 B LYS O 794 204.2 122.7 40.9 27 B LEU N 795 203.0 124.5 40.1 25 B LEU CA 795 202.7 124.9 41.5 24 B LEU CB 795 202.9 126.5 41.5 22 B LEU CG 795 204.2 127.0 41.0 21 B LEU CD1 795 204.2 128.5 40.9 19 B LEU CD2 795 205.4 126.5 41.8 22 B LEU C 795 201.3 124.5 41.8 24 B LEU O 795 200.5 124.1 41.0 26 B VAL N 796 201.0 124.7 43.1 24 B VAL CA 796 199.7 124.4 43.6 25 B VAL CB 796 199.6 124.6 45.1 26 B VAL CG1 796 199.0 123.3 45.8 25 B VAL CG2 796 200.9 125.0 45.7 28 B VAL C 796 198.7 125.5 43.0 24 B VAL O 796 199.2 126.6 42.7 25 B ASP N 797 197.5 125.1 43.0 24 B ASP CA 797 196.5 126.1 42.5 24 B ASP CB 797 196.4 126.2 41.0 24 B ASP CG 797 195.4 127.2 40.5 23 B ASP OD1 797 194.6 127.7 41.3 24 B ASP OD2 797 195.3 127.4 39.3 22 B ASP C 797 195.1 125.6 43.0 25 B ASP O 797 194.7 124.5 42.7 26 B GLY N 798 194.4 126.5 43.7 26 B GLY CA 798 193.1 126.1 44.3 26 B GLY C 798 192.1 125.5 43.4 28 B GLY O 798 191.3 124.8 43.9 30 B CYS N 799 192.1 125.9 42.1 27 B CYS CA 799 191.0 125.4 41.2 26 B CYS CB 799 190.9 126.1 39.9 25 B CYS SG 799 192.5 126.1 38.9 26 B CYS C 799 191.2 123.9 41.0 27 B CYS O 799 190.3 123.2 40.8 28 B TYR N 800 192.5 123.4 41.2 29 B TYR CA 800 192.8 122.0 41.0 32 B TYR CB 800 194.3 121.8 40.8 31 B TYR CG 800 194.6 122.3 39.4 32 B TYR CD1 800 195.4 123.4 39.2 32 B TYR CE1 800 195.7 123.9 37.9 33 B TYR CD2 800 194.1 121.6 38.3 32 B TYR CE2 800 194.4 122.1 37.0 32 B TYR CZ 800 195.1 123.2 36.8 33 B TYR OH 800 195.4 123.7 35.6 34 B TYR C 800 192.4 121.2 42.2 34 B TYR O 800 192.6 119.9 42.2 34 B SER N 801 191.8 121.8 43.2 35 B SER CA 801 191.3 121.1 44.4 34 B SER CB 801 190.8 122.2 45.4 36 B SER OG 801 191.9 123.0 45.8 36 B SER C 801 190.1 120.3 43.9 33 B SER O 801 189.7 119.3 44.5 35 B PHE N 802 189.5 120.8 42.8 32 B PHE CA 802 188.4 120.0 42.2 31 B PHE CB 802 187.2 120.9 41.7 31 B PHE CG 802 186.2 120.0 41.0 33 B PHE CD1 802 185.3 119.2 41.8 34 B PHE CD2 802 186.1 120.0 39.6 34 B PHE CE1 802 184.4 118.4 41.1 34 B PHE CE2 802 185.1 119.2 39.0 34 B PHE CZ 802 184.3 118.4 39.8 34 B PHE C 802 188.8 119.2 41.0 30 B PHE O 802 188.4 118.0 40.8 30 B TRP N 803 189.5 119.8 40.0 27 B TRP CA 803 189.9 119.1 38.8 25 B TRP CB 803 190.6 120.0 37.8 23 B TRP CG 803 189.8 121.2 37.3 20 B TRP CD2 803 188.6 121.3 36.6 18 B TRP CE2 803 188.3 122.6 36.4 18 B TRP CE3 803 187.7 120.3 36.2 18 B TRP CD1 803 190.2 122.5 37.5 18 B TRP NE1 803 189.3 123.3 36.9 19 B TRP CZ2 803 187.2 123.0 35.7 17 B TRP CZ3 803 186.5 120.7 35.5 17 B TRP CH2 803 186.3 122.1 35.2 18 B TRP C 803 190.8 117.8 39.1 26 B TRP O 803 190.6 116.8 38.5 26 B GLN N 804 191.7 117.9 40.1 26 B GLN CA 804 192.5 116.8 40.4 28 B GLN CB 804 193.9 117.3 40.9 26 B GLN CG 804 194.8 118.0 39.8 25 B GLN CD 804 195.4 117.0 38.8 25 B GLN OE1 804 194.8 116.0 38.5 25 B GLN NE2 804 196.6 117.4 38.4 24 B GLN C 804 191.9 115.9 41.6 32 B GLN O 804 191.9 114.7 41.4 32 B ALA N 805 191.5 116.5 42.7 34 B ALA CA 805 190.9 115.8 43.8 34 B ALA CB 805 190.7 116.7 45.0 35 B ALA C 805 189.6 115.1 43.4 35 B ALA O 805 189.3 114.1 43.9 37 B GLY N 806 188.9 115.8 42.5 34 B GLY CA 806 187.6 115.2 42.0 33 B GLY C 806 187.8 113.8 41.3 34 B GLY O 806 186.9 113.1 41.1 35 B LEU N 807 189.0 113.5 40.9 34 B LEU CA 807 189.4 112.3 40.1 35 B LEU CB 807 190.7 112.4 39.4 35 B LEU CG 807 190.9 113.3 38.2 35 B LEU CD1 807 192.3 113.3 37.8 35 B LEU CD2 807 190.0 112.8 37.1 33 B LEU C 807 189.4 111.0 41.0 36 B LEU O 807 189.3 109.9 40.5 38 B LEU N 808 189.5 111.2 42.3 37 B LEU CA 808 189.5 110.1 43.2 36 B LEU CB 808 190.3 110.4 44.5 35 B LEU CG 808 191.7 110.7 44.1 35 B LEU CD1 808 192.4 111.5 45.0 35 B LEU CD2 808 192.4 109.4 43.9 34 B LEU C 808 188.1 109.5 43.4 35 B LEU O 808 188.0 108.3 43.4 38 B PRO N 809 187.1 110.3 43.6 32 B PRO CD 809 187.1 111.8 44.0 31 B PRO CA 809 185.8 109.8 43.8 31 B PRO CB 809 184.9 111.0 43.9 30 B PRO CG 809 185.7 111.9 44.6 30 B PRO C 809 185.4 109.0 42.5 32 B PRO O 809 184.8 107.9 42.5 34 B LEU N 810 185.8 109.6 41.4 31 B LEU CA 810 185.5 109.0 40.1 30 B LEU CB 810 186.0 109.8 38.9 29 B LEU CG 810 185.2 111.2 38.8 29 B LEU CD1 810 185.5 111.8 37.5 29 B LEU CD2 810 183.8 110.9 39.0 28 B LEU C 810 186.3 107.6 40.0 31 B LEU O 810 185.7 106.6 39.6 30 B LEU N 811 187.5 107.7 40.5 33 B LEU CA 811 188.4 106.5 40.5 35 B LEU CB 811 189.8 106.8 40.7 32 B LEU CG 811 190.6 107.2 39.4 29 B LEU CD1 811 192.0 107.6 39.7 28 B LEU CD2 811 190.6 106.0 38.5 27 B LEU C 811 188.0 105.5 41.6 38 B LEU O 811 188.5 104.3 41.7 40 B HIS N 812 187.1 105.9 42.6 41 B HIS CA 812 186.7 105.0 43.6 43 B HIS CB 812 186.1 105.7 44.8 45 B HIS CG 812 186.4 105.1 46.1 47 B HIS CD2 812 185.8 104.3 46.9 47 B HIS ND1 812 187.7 105.4 46.7 47 B HIS CE1 812 187.8 104.8 47.8 47 B HIS NE2 812 186.7 104.0 48.0 47 B HIS C 812 185.7 104.1 42.9 45 B HIS O 812 185.9 102.9 42.8 45 B ARG N 813 184.6 104.7 42.3 47 B ARG CA 813 183.6 104.0 41.6 49 B ARG CB 813 182.7 104.9 40.8 52 B ARG CG 813 181.8 105.9 41.7 56 B ARG CD 813 181.3 107.1 40.8 59 B ARG NE 813 180.2 107.8 41.4 62 B ARG CZ 813 180.2 108.4 42.6 63 B ARG NH1 813 181.3 108.4 43.4 62 B ARG NH2 813 179.2 109.2 43.0 63 B ARG C 813 184.2 103.1 40.6 49 B ARG O 813 184.1 101.8 40.7 51 B ALA N 814 185.0 103.6 39.7 49 B ALA CA 814 185.7 102.8 38.7 49 B ALA CB 814 186.7 103.6 37.9 49 B ALA C 814 186.3 101.6 39.2 50 B ALA O 814 185.9 100.5 38.8 50 B LEU N 815 187.2 101.7 40.2 50 B LEU CA 815 187.9 100.6 40.8 51 B LEU CB 815 189.0 101.0 41.7 50 B LEU CG 815 190.1 101.8 41.0 51 B LEU CD1 815 191.2 102.2 42.0 51 B LEU CD2 815 190.7 101.0 39.9 51 B LEU C 815 187.0 99.6 41.5 52 B LEU O 815 187.1 98.4 41.4 52 B HIS N 816 186.1 100.1 42.3 52 B HIS CA 816 185.2 99.3 43.1 54 B HIS CB 816 184.4 100.1 44.0 56 B HIS CG 816 183.2 99.5 44.6 59 B HIS CD2 816 183.0 98.5 45.5 60 B HIS ND1 816 181.9 99.8 44.2 61 B HIS CE1 816 181.0 99.1 44.9 61 B HIS NE2 816 181.7 98.2 45.7 62 B HIS C 816 184.2 98.6 42.1 54 B HIS O 816 183.8 97.4 42.3 53 B ALA N 817 184.0 99.2 40.9 54 B ALA CA 817 183.2 98.7 39.9 55 B ALA CB 817 183.0 99.7 38.8 55 B ALA C 817 183.8 97.4 39.4 55 B ALA O 817 183.1 96.5 39.0 57 B GLN N 818 185.1 97.4 39.3 56 B GLN CA 818 185.7 96.1 38.9 57 B GLN CB 818 186.9 96.4 38.0 56 B GLN CG 818 188.0 97.4 38.4 56 B GLN CD 818 188.9 97.8 37.2 56 B GLN OE1 818 188.7 97.3 36.1 56 B GLN NE2 818 189.9 98.6 37.5 56 B GLN C 818 186.1 95.3 40.1 58 B GLN O 818 187.1 94.6 40.2 58 B GLY N 819 185.2 95.4 41.1 58 B GLY CA 819 185.3 94.8 42.4 58 B GLY C 819 186.6 94.8 43.1 59 B GLY O 819 187.3 93.8 43.2 60 B ASP N 820 187.1 96.0 43.5 60 B ASP CA 820 188.3 96.1 44.1 61 B ASP CB 820 189.0 97.4 43.8 62 B ASP CG 820 190.5 97.3 44.0 62 B ASP OD1 820 191.3 97.8 43.1 63 B ASP OD2 820 191.0 96.8 45.1 62 B ASP C 820 188.1 96.0 45.6 61 B ASP O 820 187.2 96.6 46.2 61 B PRO N 821 188.8 95.1 46.3 62 B PRO CD 821 189.5 94.0 45.6 63 B PRO CA 821 188.7 94.8 47.8 63 B PRO CB 821 189.3 93.4 47.9 63 B PRO CG 821 189.2 92.8 46.5 63 B PRO C 821 189.4 95.8 48.6 63 B PRO O 821 188.9 96.3 49.6 65 B ALA N 822 190.7 96.1 48.3 62 B ALA CA 822 191.6 97.0 49.0 60 B ALA CB 822 193.0 97.0 48.5 59 B ALA C 822 191.1 98.5 49.2 59 B ALA O 822 191.9 99.3 49.7 59 B LEU N 823 189.9 98.8 48.7 59 B LEU CA 823 189.4 100.2 48.8 60 B LEU CB 823 188.4 100.5 47.7 60 B LEU CG 823 188.9 100.5 46.3 60 B LEU CD1 823 187.7 100.6 45.4 59 B LEU CD2 823 189.8 101.7 46.0 60 B LEU C 823 188.8 100.5 50.2 61 B LEU O 823 188.0 99.8 50.7 62 B SER N 824 189.1 101.7 50.6 62 B SER CA 824 188.6 102.3 51.9 62 B SER CB 824 189.3 103.6 52.2 62 B SER OG 824 188.8 104.3 53.3 61 B SER C 824 187.1 102.5 51.9 63 B SER O 824 186.5 102.7 50.8 63 B MET N 825 186.5 102.4 53.1 65 B MET CA 825 185.1 102.6 53.2 66 B MET CB 825 184.4 101.4 53.9 70 B MET CG 825 184.6 100.0 53.3 74 B MET SD 825 183.9 99.9 51.6 79 B MET CE 825 182.2 99.3 52.0 78 B MET C 825 184.7 103.9 53.9 64 B MET O 825 183.5 104.1 54.2 64 B SER N 826 185.7 104.8 54.1 62 B SER CA 826 185.5 106.0 54.8 60 B SER CB 826 185.9 105.9 56.2 60 B SER OG 826 187.3 105.6 56.3 59 B SER C 826 186.2 107.3 54.1 58 B SER O 826 185.8 108.4 54.4 57 B HIS N 827 187.2 107.1 53.3 57 B HIS CA 827 188.0 108.2 52.8 54 B HIS CB 827 189.3 108.3 53.5 56 B HIS CG 827 189.1 108.7 55.0 58 B HIS CD2 827 189.6 108.2 56.1 58 B HIS ND1 827 188.4 109.8 55.4 58 B HIS CE1 827 188.4 110.0 56.7 59 B HIS NE2 827 189.2 109.0 57.2 59 B HIS C 827 188.4 108.0 51.3 51 B HIS O 827 188.4 106.9 50.8 51 B TRP N 828 188.7 109.1 50.7 46 B TRP CA 828 189.1 109.1 49.3 41 B TRP CB 828 188.9 110.5 48.6 37 B TRP CG 828 187.5 110.9 48.6 32 B TRP CD2 828 186.4 110.1 48.1 31 B TRP CE2 828 185.2 110.8 48.2 30 B TRP CE3 828 186.3 108.8 47.6 31 B TRP CD1 828 186.9 112.0 49.0 31 B TRP NE1 828 185.6 112.0 48.8 31 B TRP CZ2 828 184.0 110.4 47.8 30 B TRP CZ3 828 185.1 108.3 47.1 30 B TRP CH2 828 184.0 109.1 47.2 30 B TRP C 828 190.6 108.9 49.3 42 B TRP O 828 191.3 109.1 50.3 40 B MET N 829 191.2 108.5 48.1 42 B MET CA 829 192.6 108.2 48.1 41 B MET CB 829 192.9 107.2 47.0 42 B MET CG 829 192.2 105.8 47.3 44 B MET SD 829 192.6 104.4 46.3 46 B MET CE 829 194.4 104.5 46.4 43 B MET C 829 193.5 109.4 47.9 41 B MET O 829 194.4 109.5 47.0 41 B PHE N 830 193.3 110.4 48.8 40 B PHE CA 830 194.1 111.6 49.0 39 B PHE CB 830 193.7 112.6 47.9 35 B PHE CG 830 192.5 113.4 48.1 30 B PHE CD1 830 192.5 114.6 48.9 30 B PHE CD2 830 191.3 113.1 47.5 30 B PHE CE1 830 191.4 115.4 49.0 28 B PHE CE2 830 190.1 113.8 47.7 29 B PHE CZ 830 190.2 115.0 48.4 29 B PHE C 830 193.9 112.1 50.4 40 B PHE O 830 193.0 111.7 51.1 41 B HIS N 831 194.8 113.0 50.8 42 B HIS CA 831 194.7 113.6 52.2 42 B HIS CB 831 196.0 114.3 52.5 43 B HIS CG 831 196.4 114.2 54.0 44 B HIS CD2 831 195.8 114.7 55.1 45 B HIS ND1 831 197.5 113.5 54.5 45 B HIS CE1 831 197.5 113.6 55.8 45 B HIS NE2 831 196.5 114.3 56.2 46 B HIS C 831 193.6 114.6 52.2 42 B HIS O 831 193.8 115.8 51.9 42 B GLN N 832 192.4 114.2 52.6 43 B GLN CA 832 191.2 115.1 52.7 45 B GLN CB 832 190.0 114.4 53.2 45 B GLN CG 832 189.3 113.5 52.1 45 B GLN CD 832 189.1 112.1 52.5 45 B GLN OE1 832 188.0 111.7 52.6 44 B GLN NE2 832 190.2 111.4 52.7 44 B GLN C 832 191.5 116.2 53.7 46 B GLN O 832 191.0 117.4 53.5 46 B GLN N 833 192.2 115.9 54.8 48 B GLN CA 833 192.5 116.9 55.8 49 B GLN CB 833 193.2 116.3 57.0 52 B GLN CG 833 193.3 117.2 58.2 55 B GLN CD 833 194.4 116.7 59.1 57 B GLN OE1 833 195.1 115.7 58.9 58 B GLN NE2 833 194.6 117.5 60.2 57 B GLN C 833 193.4 118.0 55.2 48 B GLN O 833 193.0 119.2 55.2 48 B ALA N 834 194.5 117.7 54.7 46 B ALA CA 834 195.5 118.6 54.1 44 B ALA CB 834 196.7 117.8 53.5 42 B ALA C 834 194.9 119.5 53.0 44 B ALA O 834 195.1 120.7 53.0 45 B LEU N 835 194.0 119.0 52.1 43 B LEU CA 835 193.4 119.8 51.1 42 B LEU CB 835 192.6 118.9 50.1 42 B LEU CG 835 191.9 119.8 49.0 41 B LEU CD1 835 192.9 120.5 48.2 40 B LEU CD2 835 190.9 119.0 48.2 39 B LEU C 835 192.4 120.8 51.7 43 B LEU O 835 192.2 121.9 51.2 44 B GLN N 836 191.7 120.5 52.8 42 B GLN CA 836 190.8 121.4 53.5 40 B GLN CB 836 189.9 120.6 54.4 40 B GLN CG 836 189.0 119.7 53.8 40 B GLN CD 836 188.0 119.1 54.7 41 B GLN OE1 836 187.2 119.8 55.4 41 B GLN NE2 836 188.1 117.8 54.9 42 B GLN C 836 191.5 122.5 54.2 39 B GLN O 836 191.1 123.6 54.4 38 B GLU N 837 192.7 122.2 54.7 38 B GLU CA 837 193.6 123.1 55.4 37 B GLU CB 837 194.7 122.5 56.2 37 B GLU CG 837 194.1 121.7 57.3 37 B GLU CD 837 195.1 121.0 58.3 37 B GLU OE1 837 196.3 121.2 58.1 37 B GLU OE2 837 194.6 120.3 59.1 38 B GLU C 837 194.1 124.1 54.4 37 B GLU O 837 193.9 125.3 54.6 38 B TYR N 838 194.6 123.6 53.3 37 B TYR CA 838 195.1 124.5 52.2 35 B TYR CB 838 195.5 123.7 50.9 36 B TYR CG 838 196.0 124.6 49.8 35 B TYR CD1 838 197.3 125.2 49.9 36 B TYR CE1 838 197.7 126.2 49.0 35 B TYR CD2 838 195.2 125.0 48.8 35 B TYR CE2 838 195.6 126.0 47.8 34 B TYR CZ 838 196.8 126.6 48.0 34 B TYR OH 838 197.3 127.6 47.1 32 B TYR C 838 194.0 125.5 51.8 34 B TYR O 838 194.3 126.7 51.9 34 B ILE N 839 192.9 125.0 51.4 32 B ILE CA 839 191.8 125.9 51.0 31 B ILE CB 839 190.6 125.0 50.5 29 B ILE CG2 839 189.4 126.0 50.0 28 B ILE CG1 839 191.0 124.1 49.4 28 B ILE CD1 839 189.9 123.4 48.7 28 B ILE C 839 191.3 126.9 52.1 34 B ILE O 839 191.3 128.1 51.8 36 B LEU N 840 190.9 126.4 53.2 33 B LEU CA 840 190.5 127.2 54.3 32 B LEU CB 840 190.1 126.4 55.5 30 B LEU CG 840 188.9 125.5 55.3 29 B LEU CD1 840 188.8 124.5 56.4 28 B LEU CD2 840 187.6 126.3 55.2 28 B LEU C 840 191.5 128.3 54.8 32 B LEU O 840 191.2 129.4 54.9 33 B MET N 841 192.8 127.8 54.9 33 B MET CA 841 193.8 128.7 55.4 34 B MET CB 841 195.0 128.0 56.0 35 B MET CG 841 194.7 127.4 57.5 37 B MET SD 841 196.2 126.8 58.3 40 B MET CE 841 195.9 125.0 58.3 39 B MET C 841 194.4 129.6 54.3 36 B MET O 841 194.6 130.8 54.5 36 B CYS N 842 194.8 129.0 53.1 36 B CYS CA 842 195.4 129.7 52.0 34 B CYS CB 842 196.6 128.9 51.5 33 B CYS SG 842 197.7 128.2 52.7 34 B CYS C 842 194.6 130.3 50.9 34 B CYS O 842 195.1 131.3 50.3 36 B CYS N 843 193.5 129.7 50.5 34 B CYS CA 843 192.7 130.2 49.4 33 B CYS CB 843 192.3 129.0 48.5 32 B CYS SG 843 193.6 127.9 48.1 33 B CYS C 843 191.4 131.0 49.6 33 B CYS O 843 190.6 131.2 48.7 33 B GLN N 844 191.3 131.6 50.8 35 B GLN CA 844 190.1 132.4 51.1 37 B GLN CB 844 189.6 132.0 52.4 37 B GLN CG 844 188.1 132.1 52.6 37 B GLN CD 844 187.6 131.1 53.6 37 B GLN OE1 844 186.4 130.9 53.7 38 B GLN NE2 844 188.5 130.5 54.4 35 B GLN C 844 190.4 133.9 51.0 37 B GLN O 844 191.4 134.4 51.5 38 B CYS N 845 189.5 134.7 50.4 37 B CYS CA 845 189.7 136.1 50.3 39 B CYS CB 845 189.2 136.7 49.0 39 B CYS SG 845 189.4 138.5 48.9 39 B CYS C 845 188.9 136.8 51.4 40 B CYS O 845 187.7 136.5 51.5 41 B PRO N 846 189.5 137.6 52.3 41 B PRO CD 846 190.9 138.0 52.2 41 B PRO CA 846 188.9 138.3 53.4 41 B PRO CB 846 189.9 139.3 53.8 41 B PRO CG 846 191.2 138.5 53.6 40 B PRO C 846 187.6 139.0 53.0 42 B PRO O 846 186.5 138.8 53.6 43 B ALA N 847 187.7 139.7 51.9 41 B ALA CA 847 186.5 140.4 51.3 40 B ALA CB 847 187.0 141.4 50.3 40 B ALA C 847 185.5 139.5 50.6 39 B ALA O 847 184.5 140.0 50.2 41 B GLY N 848 185.8 138.2 50.6 38 B GLY CA 848 184.8 137.3 49.9 38 B GLY C 848 185.5 136.7 48.7 37 B GLY O 848 186.3 137.3 48.1 38 B GLY N 849 185.1 135.5 48.3 35 B GLY CA 849 185.6 134.9 47.1 32 B GLY C 849 186.9 134.1 47.5 31 B GLY O 849 187.5 134.4 48.5 29 B LEU N 850 187.2 133.1 46.7 30 B LEU CA 850 188.4 132.3 46.9 28 B LEU CB 850 188.0 130.8 47.0 29 B LEU CG 850 187.2 130.1 48.1 30 B LEU CD1 850 188.0 130.0 49.3 30 B LEU CD2 850 185.9 130.8 48.3 30 B LEU C 850 189.4 132.5 45.8 28 B LEU O 850 189.1 133.2 44.8 27 B LEU N 851 190.6 131.9 46.0 28 B LEU CA 851 191.6 132.2 45.0 29 B LEU CB 851 192.3 133.5 45.3 31 B LEU CG 851 192.5 133.7 46.8 32 B LEU CD1 851 193.8 133.2 47.3 34 B LEU CD2 851 192.4 135.2 47.1 32 B LEU C 851 192.6 131.1 44.7 31 B LEU O 851 192.6 130.1 45.4 32 B ASP N 852 193.4 131.3 43.7 30 B ASP CA 852 194.5 130.4 43.3 30 B ASP CB 852 195.3 131.1 42.2 31 B ASP CG 852 196.5 130.3 41.7 31 B ASP OD1 852 197.1 129.5 42.5 32 B ASP OD2 852 196.9 130.5 40.6 32 B ASP C 852 195.3 130.1 44.5 30 B ASP O 852 195.4 128.9 44.9 31 B LYS N 853 196.1 131.0 45.0 31 B LYS CA 853 196.9 130.8 46.1 31 B LYS CB 853 198.3 130.3 45.6 29 B LYS CG 853 199.0 131.2 44.7 27 B LYS CD 853 200.4 130.7 44.5 27 B LYS CE 853 200.4 129.3 43.9 28 B LYS NZ 853 199.9 129.1 42.6 27 B LYS C 853 197.1 132.2 46.7 33 B LYS O 853 196.6 133.2 46.1 33 B PRO N 854 197.8 132.3 47.9 36 B PRO CD 854 198.3 131.2 48.7 37 B PRO CA 854 198.0 133.6 48.5 38 B PRO CB 854 198.8 133.3 49.7 38 B PRO CG 854 199.4 132.0 49.4 37 B PRO C 854 198.7 134.7 47.5 39 B PRO O 854 199.7 134.4 46.9 40 B GLY N 855 198.1 135.9 47.4 40 B GLY CA 855 198.6 136.9 46.6 40 B GLY C 855 197.8 137.1 45.3 41 B GLY O 855 197.5 138.2 44.9 43 B LYS N 856 197.3 135.9 44.8 40 B LYS CA 856 196.5 135.9 43.6 39 B LYS CB 856 196.2 134.4 43.2 39 B LYS CG 856 197.5 133.6 42.9 38 B LYS CD 856 198.0 134.2 41.6 40 B LYS CE 856 199.1 133.3 41.0 40 B LYS NZ 856 199.3 133.6 39.6 42 B LYS C 856 195.2 136.6 43.8 39 B LYS O 856 194.7 136.7 45.0 40 B SER N 857 194.6 137.1 42.8 40 B SER CA 857 193.3 137.8 43.0 41 B SER CB 857 193.1 138.8 41.9 43 B SER OG 857 194.0 139.9 41.9 46 B SER C 857 192.1 136.8 43.0 41 B SER O 857 192.3 135.7 42.5 41 B ARG N 858 191.0 137.3 43.5 40 B ARG CA 858 189.8 136.5 43.6 39 B ARG CB 858 188.9 136.9 44.8 39 B ARG CG 858 188.1 138.1 44.5 39 B ARG CD 858 187.5 138.7 45.7 39 B ARG NE 858 186.7 139.9 45.4 40 B ARG CZ 858 186.1 140.6 46.4 40 B ARG NH1 858 186.2 140.3 47.6 41 B ARG NH2 858 185.3 141.7 46.0 40 B ARG C 858 189.0 136.6 42.3 37 B ARG O 858 189.0 137.6 41.6 38 B ASP N 859 188.2 135.5 42.1 34 B ASP CA 859 187.3 135.4 41.0 31 B ASP CB 859 188.1 135.3 39.6 31 B ASP CG 859 189.0 134.0 39.6 31 B ASP OD1 859 188.5 132.9 39.4 31 B ASP OD2 859 190.2 134.2 39.8 33 B ASP C 859 186.4 134.3 41.2 30 B ASP O 859 186.6 133.4 42.0 28 B PHE N 860 185.3 134.3 40.4 30 B PHE CA 860 184.2 133.3 40.5 29 B PHE CB 860 183.0 133.7 39.7 29 B PHE CG 860 182.6 135.1 40.1 30 B PHE CD1 860 182.7 136.2 39.1 31 B PHE CD2 860 182.3 135.4 41.4 30 B PHE CE1 860 182.4 137.5 39.5 30 B PHE CE2 860 182.0 136.7 41.8 30 B PHE CZ 860 182.0 137.8 40.8 30 B PHE C 860 184.6 131.9 40.1 28 B PHE O 860 184.1 130.9 40.6 31 B TYR N 861 185.7 131.8 39.3 26 B TYR CA 861 186.1 130.4 38.8 23 B TYR CB 861 187.1 130.6 37.6 22 B TYR CG 861 187.9 129.4 37.3 19 B TYR CD1 861 187.4 128.3 36.6 19 B TYR CE1 861 188.2 127.2 36.4 18 B TYR CD2 861 189.2 129.4 37.8 18 B TYR CE2 861 190.0 128.3 37.6 18 B TYR CZ 861 189.5 127.2 36.9 17 B TYR OH 861 190.3 126.1 36.8 19 B TYR C 861 186.8 129.7 39.9 23 B TYR O 861 186.5 128.6 40.2 23 B HIS N 862 187.7 130.4 40.6 25 B HIS CA 862 188.4 129.8 41.8 25 B HIS CB 862 189.6 130.6 42.2 23 B HIS CG 862 190.7 130.5 41.2 23 B HIS CD2 862 191.7 129.5 41.1 22 B HIS ND1 862 191.0 131.4 40.3 24 B HIS CE1 862 192.0 131.1 39.5 25 B HIS NE2 862 192.5 129.9 40.0 23 B HIS C 862 187.4 129.6 43.0 27 B HIS O 862 187.6 128.8 43.8 28 B THR N 863 186.5 130.6 43.0 30 B THR CA 863 185.5 130.5 44.1 32 B THR CB 863 184.5 131.8 44.1 32 B THR OG1 863 185.3 133.0 44.5 32 B THR CG2 863 183.4 131.7 45.1 33 B THR C 863 184.7 129.2 43.9 31 B THR O 863 184.6 128.4 44.8 34 B CYS N 864 184.2 129.0 42.7 30 B CYS CA 864 183.5 127.9 42.3 29 B CYS CB 864 183.0 127.9 40.9 30 B CYS SG 864 182.4 126.4 40.1 30 B CYS C 864 184.3 126.6 42.5 29 B CYS O 864 183.7 125.6 43.0 31 B TYR N 865 185.6 126.6 42.2 28 B TYR CA 865 186.4 125.4 42.3 28 B TYR CB 865 187.3 125.2 41.1 26 B TYR CG 865 186.5 125.0 39.8 25 B TYR CD1 865 186.3 126.0 38.8 25 B TYR CE1 865 185.5 125.7 37.7 25 B TYR CD2 865 185.9 123.8 39.6 24 B TYR CE2 865 185.0 123.5 38.5 24 B TYR CZ 865 184.8 124.5 37.6 25 B TYR OH 865 184.0 124.3 36.5 26 B TYR C 865 187.0 125.1 43.6 29 B TYR O 865 187.3 123.9 43.9 29 B CYS N 866 187.4 126.1 44.4 29 B CYS CA 866 188.0 125.8 45.7 29 B CYS CB 866 188.5 127.1 46.3 29 B CYS SG 866 190.1 127.7 45.7 30 B CYS C 866 186.8 125.3 46.6 29 B CYS O 866 187.0 124.4 47.4 29 B LEU N 867 185.6 125.9 46.4 27 B LEU CA 867 184.5 125.4 47.2 29 B LEU CB 867 183.3 126.3 47.0 26 B LEU CG 867 183.5 127.7 47.7 25 B LEU CD1 867 182.3 128.6 47.5 25 B LEU CD2 867 183.7 127.5 49.1 25 B LEU C 867 184.1 123.9 46.7 32 B LEU O 867 183.9 123.1 47.6 33 B SER N 868 184.1 123.7 45.4 34 B SER CA 868 183.8 122.3 44.9 33 B SER CB 868 183.8 122.3 43.4 33 B SER OG 868 182.7 123.0 42.8 32 B SER C 868 184.8 121.3 45.5 33 B SER O 868 184.4 120.2 45.8 34 B GLY N 869 186.0 121.7 45.6 34 B GLY CA 869 187.1 120.9 46.1 35 B GLY C 869 187.0 120.6 47.6 36 B GLY O 869 187.3 119.5 48.1 37 B LEU N 870 186.5 121.6 48.3 35 B LEU CA 870 186.4 121.5 49.8 34 B LEU CB 870 185.9 122.9 50.4 32 B LEU CG 870 185.8 123.0 51.9 32 B LEU CD1 870 187.2 122.6 52.5 30 B LEU CD2 870 185.4 124.4 52.3 30 B LEU C 870 185.3 120.5 50.1 34 B LEU O 870 185.5 119.5 50.8 32 B SER N 871 184.2 120.6 49.3 36 B SER CA 871 183.1 119.7 49.4 38 B SER CB 871 182.0 120.1 48.5 38 B SER OG 871 180.8 119.3 48.7 39 B SER C 871 183.5 118.2 49.0 39 B SER O 871 183.0 117.3 49.6 41 B ILE N 872 184.4 118.1 48.0 40 B ILE CA 872 184.8 116.8 47.7 40 B ILE CB 872 185.8 116.7 46.4 38 B ILE CG2 872 186.5 115.4 46.3 36 B ILE CG1 872 185.0 117.0 45.1 38 B ILE CD1 872 184.0 115.8 44.7 38 B ILE C 872 185.6 116.2 48.9 41 B ILE O 872 185.2 115.2 49.4 43 B ALA N 873 186.5 117.0 49.4 44 B ALA CA 873 187.3 116.7 50.6 46 B ALA CB 873 188.3 117.8 50.8 47 B ALA C 873 186.5 116.4 51.9 46 B ALA O 873 186.9 115.6 52.7 45 B GLN N 874 185.4 117.0 52.1 48 B GLN CA 874 184.6 116.8 53.3 50 B GLN CB 874 183.7 118.1 53.6 49 B GLN CG 874 184.4 119.3 53.9 47 B GLN CD 874 183.4 120.5 53.9 47 B GLN OE1 874 182.3 120.4 53.2 47 B GLN NE2 874 183.7 121.6 54.5 47 B GLN C 874 183.6 115.7 53.2 51 B GLN O 874 183.1 115.2 54.2 53 B HIS N 875 183.3 115.2 52.0 52 B HIS CA 875 182.3 114.1 51.9 53 B HIS CB 875 181.0 114.7 51.3 53 B HIS CG 875 180.6 116.0 51.9 52 B HIS CD2 875 180.8 117.3 51.5 53 B HIS ND1 875 179.8 116.0 53.0 53 B HIS CE1 875 179.5 117.3 53.2 52 B HIS NE2 875 180.1 118.1 52.4 53 B HIS C 875 182.7 112.9 51.1 55 B HIS O 875 183.0 112.9 49.9 55 B PHE N 876 182.7 111.8 51.9 57 B PHE CA 876 183.0 110.5 51.3 59 B PHE CB 876 184.0 109.7 52.1 57 B PHE CG 876 184.3 108.3 51.6 57 B PHE CD1 876 185.2 108.1 50.6 56 B PHE CD2 876 183.6 107.2 52.1 56 B PHE CE1 876 185.5 106.8 50.1 56 B PHE CE2 876 183.8 106.0 51.6 56 B PHE CZ 876 184.7 105.7 50.6 56 B PHE C 876 181.7 109.6 51.1 61 B PHE O 876 180.7 109.9 51.8 61 B GLY N 877 181.8 108.7 50.2 64 B GLY CA 877 180.7 107.8 50.0 68 B GLY C 877 181.2 106.5 49.4 71 B GLY O 877 182.4 106.5 49.0 72 B SER N 878 180.5 105.4 49.5 73 B SER CA 878 181.0 104.1 49.0 74 B SER CB 878 182.2 103.6 49.7 74 B SER OG 878 182.7 102.3 49.2 74 B SER C 878 179.8 103.0 49.1 75 B SER O 878 180.0 101.9 49.6 76 B GLY N 879 178.7 103.4 48.6 76 B GLY CA 879 177.5 102.5 48.6 77 B GLY C 879 176.5 103.1 49.6 77 B GLY O 879 175.6 103.8 49.3 77 B ALA N 880 176.8 102.8 50.9 78 B ALA CA 880 176.0 103.3 52.0 77 B ALA CB 880 175.1 102.1 52.5 78 B ALA C 880 176.9 103.8 53.1 77 B ALA O 880 176.5 104.0 54.2 77 B MET N 881 178.2 103.9 52.8 76 B MET CA 881 179.2 104.4 53.7 75 B MET CB 881 180.6 104.0 53.3 76 B MET CG 881 180.7 102.6 52.8 77 B MET SD 881 180.8 101.4 54.2 78 B MET CE 881 179.1 101.1 54.5 78 B MET C 881 179.1 106.0 53.6 73 B MET O 881 178.8 106.5 52.5 73 B LEU N 882 179.3 106.7 54.7 72 B LEU CA 882 179.2 108.1 54.7 71 B LEU CB 882 177.7 108.6 54.9 72 B LEU CG 882 177.0 109.3 53.8 73 B LEU CD1 882 177.8 110.5 53.3 74 B LEU CD2 882 176.6 108.4 52.7 73 B LEU C 882 180.1 108.9 55.7 70 B LEU O 882 179.6 109.5 56.6 71 B HIS N 883 181.4 108.8 55.5 68 B HIS CA 883 182.4 109.5 56.3 66 B HIS CB 883 183.6 108.6 56.6 66 B HIS CG 883 184.5 109.1 57.6 67 B HIS CD2 883 185.4 108.4 58.4 67 B HIS ND1 883 184.7 110.4 58.0 67 B HIS CE1 883 185.6 110.5 58.9 67 B HIS NE2 883 186.0 109.3 59.2 67 B HIS C 883 182.8 110.9 55.9 64 B HIS O 883 183.9 111.1 55.3 64 B ASP N 884 182.0 111.8 S6.4 61 B ASP CA 884 182.3 113.2 56.1 59 B ASP CB 884 181.0 114.1 56.3 59 B ASP CG 884 179.9 113.7 55.3 60 B ASP OD1 884 178.8 114.2 55.5 59 B ASP OD2 884 180.1 112.7 54.5 60 B ASP C 884 183.4 113.7 57.1 57 B ASP O 884 183.5 113.2 58.2 56 B VAL N 885 184.3 114.6 56.6 55 B VAL CA 885 185.4 115.1 57.4 53 B VAL CB 885 186.7 114.7 56.8 52 B VAL CG1 885 187.9 115.3 57.5 51 B VAL CG2 885 186.8 113.2 56.8 52 B VAL C 885 185.3 116.6 57.3 52 B VAL O 885 185.6 117.2 56.2 52 B VAL N 886 184.8 117.3 58.3 50 B VAL CA 886 184.7 118.7 58.3 51 B VAL CB 886 183.4 119.3 58.7 51 B VAL CG1 886 183.3 120.8 58.5 49 B VAL CG2 886 182.3 118.6 57.8 50 B VAL C 886 185.8 119.4 59.1 53 B VAL O 886 185.8 119.3 60.3 54 B MET N 887 186.7 120.1 58.4 54 B MET CA 887 187.8 120.8 59.1 53 B MET CB 887 188.9 121.1 58.1 53 B MET CG 887 190.2 120.6 58.5 53 B MET SD 887 190.1 118.9 59.0 52 B MET CE 887 191.4 118.9 60.2 53 B MET C 887 187.3 122.1 59.7 54 B MET O 887 186.5 122.9 59.1 52 B GLY N 888 187.7 122.4 61.0 55 B GLY CA 888 187.3 123.5 61.7 57 B GLY C 888 185.9 123.6 62.1 57 B GLY O 888 185.1 122.6 62.2 56 B VAL N 889 185.4 124.9 62.3 58 B VAL CA 889 184.0 125.2 62.6 58 B VAL CB 889 183.8 126.7 62.4 58 B VAL CG1 889 182.4 127.1 62.6 59 B VAL CG2 889 184.7 127.4 63.4 57 B VAL C 889 183.1 124.3 61.7 59 B VAL O 889 183.1 124.5 60.5 60 B PRO N 890 182.3 123.4 62.3 61 B PRO CD 890 182.0 123.4 63.8 62 B PRO CA 890 181.4 122.5 61.6 62 B PRO CB 890 180.7 121.8 62.8 62 B PRO CG 890 180.6 122.9 63.8 62 B PRO C 890 180.4 123.2 60.7 62 B PRO O 890 179.6 122.6 60.0 63 B GLU N 891 180.4 124.6 60.8 63 B GLU CA 891 179.5 125.4 59.9 63 B GLU CB 891 179.3 126.8 60.5 66 B GLU CG 891 178.3 126.9 61.6 70 B GLU CD 891 178.6 126.1 62.9 72 B GLU OE1 891 179.7 126.2 63.4 72 B GLU OE2 891 177.7 125.4 63.4 74 B GLU C 891 180.2 125.5 58.6 61 B GLU O 891 179.7 126.1 57.6 61 B ASN N 892 181.4 124.9 58.5 59 B ASN CA 892 182.3 124.9 57.3 56 B ASN CB 892 183.8 124.7 57.6 53 B ASN CG 892 184.3 125.9 58.5 50 B ASN OD1 892 185.4 125.8 59.0 49 B ASN ND2 892 183.6 127.0 58.5 49 B ASN C 892 181.8 123.9 56.3 56 B ASN O 892 182.2 123.9 55.1 57 B VAL N 893 181.0 122.9 56.7 55 B VAL CA 893 180.5 121.8 55.8 54 B VAL CB 893 179.8 120.8 56.5 54 B VAL CG1 893 178.5 121.4 57.2 54 B VAL CG2 893 179.4 119.7 55.6 53 B VAL C 893 179.7 122.4 54.7 54 B VAL O 893 178.8 123.2 54.9 54 B LEU N 894 179.9 121.9 53.5 53 B LEU CA 894 179.2 122.3 52.3 52 B LEU CB 894 180.2 122.6 51.2 52 B LEU CG 894 181.4 123.6 51.4 51 B LEU CD1 894 182.4 123.6 50.3 50 B LEU CD2 894 180.8 125.0 51.7 51 B LEU C 894 178.3 121.3 51.7 51 B LEU O 894 178.4 120.1 52.1 50 B GLN N 895 177.3 121.7 51.0 51 B GLN CA 895 176.4 120.8 50.3 50 B GLN CB 895 175.3 121.6 49.5 52 B GLN CG 895 174.3 122.3 50.4 55 B GLN CD 895 173.7 121.3 51.5 56 B GLN OE1 895 172.8 120.6 51.3 56 B GLN NE2 895 174.3 121.4 52.7 57 B GLN C 895 177.2 119.9 49.4 49 B GLN O 895 178.3 120.3 49.0 50 B PRO N 896 176.7 118.7 49.1 47 B PRO CD 896 175.4 118.1 49.7 46 B PRO CA 896 177.4 117.8 48.3 46 B PRO CB 896 176.7 116.5 48.5 47 B PRO CG 896 175.9 116.7 49.8 47 B PRO C 896 177.4 118.2 46.8 45 B PRO O 896 176.5 118.9 46.3 45 B THR N 897 178.4 117.7 46.1 42 B THR CA 897 178.5 117.9 44.7 40 B THR CB 897 179.6 119.0 44.3 39 B THR OG1 897 179.3 119.5 43.0 39 B THR CG2 897 181.0 118.5 44.5 38 B THR C 897 178.8 116.6 44.0 39 B THR O 897 179.5 115.7 44.5 39 B HIS N 898 178.3 116.4 42.8 39 B HIS CA 898 178.4 115.2 42.0 38 B HIS CB 898 177.3 115.1 40.9 38 B HIS CG 898 177.2 113.8 40.3 39 B HIS CD2 898 176.1 113.2 39.8 40 B HIS ND1 898 178.2 112.9 40.1 40 B HIS CE1 898 177.7 111.8 39.5 39 B HIS NE2 898 176.4 111.9 39.4 40 B HIS C 898 179.8 115.2 41.3 38 B HIS O 898 180.1 116.1 40.5 38 B PRO N 899 180.7 114.2 41.6 37 B PRO CD 899 180.5 113.0 42.5 38 B PRO CA 899 182.0 114.2 41.0 36 B PRO CB 899 182.7 113.0 41.7 37 B PRO CG 899 181.6 112.1 42.0 37 B PRO C 899 182.2 114.0 39.5 35 B PRO O 899 183.3 113.9 38.9 36 B VAL N 900 181.1 114.1 38.7 32 B VAL CA 900 181.1 114.0 37.3 30 B VAL CB 900 180.3 112.8 36.8 29 B VAL CG1 900 180.2 112.8 35.3 28 B VAL CG2 900 180.9 111.5 37.2 27 B VAL C 900 180.6 115.3 36.7 31 B VAL O 900 181.3 115.9 35.8 32 B TYR N 901 179.4 115.8 37.2 30 B TYR CA 901 178.8 117.0 36.7 30 B TYR CB 901 177.3 116.8 36.7 30 B TYR CG 901 176.9 115.7 35.8 30 B TYR CD1 901 176.6 114.4 36.4 29 B TYR CE1 901 176.2 113.4 35.6 30 B TYR CD2 901 176.8 115.8 34.5 30 B TYR CE2 901 176.4 114.8 33.6 31 B TYR CZ 901 176.1 113.6 34.2 31 B TYR OH 901 175.7 112.5 33.4 32 B TYR C 901 179.2 118.2 37.4 31 B TYR O 901 179.2 119.3 36.9 32 B ASN N 902 179.7 118.1 38.6 31 B ASN CA 902 180.0 119.2 39.5 31 B ASN CB 902 181.2 120.0 39.0 32 B ASN CG 902 181.7 120.9 40.1 32 B ASN OD1 902 181.7 120.6 41.3 33 B ASN ND2 902 182.2 122.0 39.7 32 B ASN C 902 178.8 120.0 39.8 31 B ASN O 902 178.9 121.3 39.6 30 B ILE N 903 177.7 119.4 40.0 33 B ILE CA 903 176.5 120.0 40.4 34 B ILE CB 903 175.4 120.2 39.3 32 B ILE CG2 903 175.8 121.2 38.3 32 B ILE CG1 903 175.0 118.9 38.7 31 B ILE CD1 903 173.7 119.0 37.8 27 B ILE C 903 175.9 119.1 41.5 35 B ILE O 903 176.2 117.9 41.4 35 B GLY N 904 175.2 119.6 42.4 37 B GLY CA 904 174.6 118.8 43.5 38 B GLY C 904 174.0 117.5 43.0 39 B GLY O 904 173.2 117.5 42.1 39 B PRO N 905 174.4 116.4 43.6 39 B PRO CD 905 175.3 116.3 44.7 39 B PRO CA 905 173.9 115.0 43.2 40 B PRO CB 905 174.5 114.2 44.3 40 B PRO CG 905 174.8 115.1 45.4 40 B PRO C 905 172.4 114.9 43.1 41 B PRO O 905 171.9 114.1 42.3 41 B ASP N 906 171.7 115.8 43.8 42 B ASP CA 906 170.3 115.8 43.7 44 B ASP CB 906 169.7 116.5 45.0 49 B ASP CG 906 170.3 117.9 45.2 52 B ASP OD1 906 171.3 118.0 46.1 54 B ASP OD2 906 169.9 118.9 44.6 53 B ASP C 906 169.7 116.5 42.5 43 B ASP O 906 168.7 116.0 42.0 43 B LYS N 907 170.4 117.5 42.0 42 B LYS CA 907 170.0 118.2 40.8 40 B LYS CB 907 170.9 119.5 40.6 39 B LYS CG 907 170.6 120.5 41.7 39 B LYS CD 907 169.2 121.0 41.5 41 B LYS CE 907 168.6 121.6 42.8 42 B LYS NZ 907 169.4 122.7 43.4 43 B LYS C 907 170.3 117.3 39.6 39 B LYS O 907 169.6 117.4 38.6 38 B VAL N 908 171.4 116.5 39.7 39 B VAL CA 908 171.8 115.6 38.6 40 B VAL CB 908 173.0 114.8 39.0 40 B VAL CG1 908 173.4 113.8 38.0 41 B VAL CG2 908 174.2 115.8 39.2 40 B VAL C 908 170.6 114.6 38.5 42 B VAL O 908 170.0 114.5 37.5 43 B ILE N 909 170.3 113.9 39.6 43 B ILE CA 909 169.3 112.9 39.6 45 B ILE CB 909 169.0 112.3 41.0 44 B ILE CG2 909 167.7 111.5 41.0 44 B ILE CG1 909 170.2 111.4 41.4 44 B ILE CD1 909 170.2 110.9 42.8 43 B ILE C 909 167.9 113.5 39.1 46 B ILE O 909 167.2 112.9 38.3 48 B GLN N 910 167.6 114.7 39.7 47 B GLN CA 910 166.4 115.3 39.3 49 B GLN CB 910 166.2 116.6 40.2 50 B GLN CG 910 164.9 117.4 40.0 52 B GLN CD 910 164.9 118.6 40.8 53 B GLN OE1 910 164.4 119.7 40.3 54 B GLN NE2 910 165.4 118.6 42.0 55 B GLN C 910 166.3 115.7 37.8 50 B GLN O 910 165.2 115.5 37.2 50 B ALA N 911 167.4 116.2 37.2 49 B ALA CA 911 167.4 116.5 35.8 49 B ALA CB 911 168.7 117.4 35.5 49 B ALA C 911 167.4 115.3 34.9 48 B ALA O 911 166.5 115.3 34.0 48 B THR N 912 168.3 114.4 35.1 48 B THR CA 912 168.3 113.2 34.2 50 B THR CB 912 169.3 112.1 34.6 49 B THR OG1 912 168.9 111.5 35.8 51 B THR CG2 912 170.7 112.8 34.9 48 B THR C 912 166.9 112.5 34.1 50 B THR O 912 166.4 112.2 33.0 52 B THR N 913 166.3 112.3 35.2 50 B THR CA 913 165.0 111.6 35.2 50 B THR CB 913 164.5 111.3 36.7 51 B THR OG1 913 164.3 112.5 37.4 53 B THR CG2 913 165.6 110.5 37.4 51 B THR C 913 163.9 112.4 34.5 48 B THR O 913 163.1 111.9 33.9 49 B HIS N 914 164.0 113.8 34.7 47 B HIS CA 914 163.0 114.6 34.1 45 B HIS CB 914 163.1 116.1 34.5 44 B HIS CG 914 162.4 117.0 33.6 44 B HIS CD2 914 161.1 117.4 33.6 44 B HIS ND1 914 163.0 117.5 32.5 44 B HIS CE1 914 162.1 118.3 31.8 44 B HIS NE2 914 160.9 118.2 32.5 44 B HIS C 914 163.1 114.5 32.5 45 B HIS O 914 162.1 114.6 31.8 44 B PHE N 915 164.3 114.5 32.0 46 B PHE CA 915 164.5 114.5 30.6 46 B PHE CB 915 165.9 115.0 30.3 44 B PHE CG 915 166.0 116.5 30.3 42 B PHE CD1 915 166.7 117.1 31.4 41 B PHE CD2 915 165.5 117.2 29.3 41 B PHE CE1 915 166.8 118.5 31.5 41 B PHE CE2 915 165.6 118.6 29.4 40 B PHE CZ 915 166.2 119.2 30.5 41 B PHE C 915 164.4 113.0 30.1 48 B PHE O 915 164.3 112.8 28.9 48 B LEU N 916 164.5 112.1 31.1 50 B LEU CA 916 164.4 110.7 30.8 53 B LEU CB 916 164.8 109.9 32.0 52 B LEU CG 916 165.6 108.6 31.7 52 B LEU CD1 916 166.4 108.8 30.4 52 B LEU CD2 916 166.5 108.4 32.9 52 B LEU C 916 162.9 110.3 30.4 55 B LEU O 916 162.7 109.3 29.7 56 B GLN N 917 161.9 111.2 30.7 58 B GLN CA 917 160.6 111.0 30.2 60 B GLN CB 917 159.6 111.5 31.3 62 B GLN CG 917 159.5 113.0 31.5 64 B GLN CD 917 159.1 113.4 32.9 65 B GLN OE1 917 159.2 112.6 33.8 66 B GLN NE2 917 158.7 114.6 33.0 65 B GLN C 917 160.3 111.6 28.9 61 B GLN O 917 159.2 111.8 28.5 62 B LYS N 918 161.4 111.9 28.2 63 B LYS CA 918 161.4 112.5 26.8 64 B LYS CB 918 162.1 113.8 26.8 64 B LYS CG 918 161.3 115.1 27.2 63 B LYS CD 918 161.1 115.1 28.7 64 B LYS CE 918 160.2 116.3 29.1 64 B LYS NZ 918 161.0 117.6 28.8 65 B LYS C 918 162.1 111.5 26.0 65 B LYS O 918 163.1 110.8 26.4 64 B PRO N 919 161.7 111.3 24.7 66 B PRO CD 919 160.5 111.8 24.0 67 B PRO CA 919 162.4 110.3 23.9 67 B PRO CB 919 161.4 110.0 22.8 67 B PRO CG 919 160.8 111.4 22.6 67 B PRO C 919 163.7 111.0 23.4 68 B PRO O 919 163.7 112.2 23.1 68 B VAL N 920 164.7 110.2 23.2 68 B VAL CA 920 166.0 110.6 22.7 70 B VAL CB 920 167.0 109.5 22.5 69 B VAL CG1 920 168.2 109.9 21.6 68 B VAL CG2 920 167.4 109.0 23.8 68 B VAL C 920 165.6 111.1 21.3 73 B VAL O 920 164.8 110.5 20.6 73 B PRO N 921 166.0 112.3 20.9 75 B PRO CD 921 166.7 113.4 21.7 75 B PRO CA 921 165.7 112.9 19.5 76 B PRO CB 921 166.4 114.2 19.6 76 B PRO CG 921 166.3 114.6 21.0 75 B PRO C 921 166.2 112.0 18.4 79 B PRO O 921 167.2 112.2 17.8 79 B GLY N 922 165.4 110.9 18.2 82 B GLY CA 922 165.7 109.9 17.2 86 B GLY C 922 165.3 110.4 15.8 89 B GLY O 922 164.2 111.0 15.6 89 B PHE N 923 166.2 110.2 14.8 92 B PHE CA 923 165.9 110.6 13.4 93 B PHE CB 923 166.3 112.1 13.2 94 B PHE CG 923 167.4 112.6 14.0 95 B PHE CD1 923 167.5 113.9 14.5 96 B PHE CD2 923 168.5 111.7 14.3 95 B PHE CE1 923 168.6 114.4 15.2 96 B PHE CE2 923 169.6 112.2 15.1 95 B PHE CZ 923 169.7 113.6 15.5 96 B PHE C 923 166.6 109.7 12.4 94 B PHE OT1 923 166.2 109.8 11.2 94 B PHE OT2 923 167.5 108.9 12.7 94 B ZIN ZN 1000 193.5 128.0 39.2 30 Z HFP P1 2001 197.8 126.1 32.7 41 H HFP C1 2001 197.2 125.9 30.9 42 H HFP C2 2001 195.7 125.6 31.0 40 H HFP O1 2001 198.9 126.9 32.6 42 H HFP O2 2001 198.1 124.7 33.2 41 H HFP O9 2001 197.4 127.1 30.2 44 H HFP C3 2001 195.1 124.8 30.1 36 H HFP C5 2001 193.6 124.5 30.1 34 H HFP C6 2001 193.1 124.2 31.6 31 H HFP C7 2001 191.9 123.4 31.6 29 H HFP C8 2001 191.1 123.3 32.7 26 H HFP C10 2001 189.8 122.4 32.7 22 H HFP C4 2001 195.9 124.1 28.9 35 H HFP C11 2001 188.8 122.9 31.8 20 H HFP C12 2001 187.5 122.1 31.9 19 H HFP C13 2001 186.3 122.4 31.3 19 H HFP C14 2001 186.2 123.6 30.4 18 H HFP C15 2001 185.1 121.5 31.6 18 H HFP O3 2001 196.6 126.7 33.5 41 H HFP C9 2001 191.4 124.1 33.9 25 H HOH OH2 1001 195.3 125.2 22.4 19 W HOH OH2 1002 205.3 121.6 32.9 14 W HOH OH2 1003 198.6 118.6 19.3 18 W HOH OH2 1004 200.1 127.0 30.2 16 W HOH OH2 1005 197.3 135.0 28.0 21 W HOH OH2 1006 194.1 124.4 18.1 17 W HOH OH2 1007 190.0 131.1 16.9 17 W HOH OH2 1008 192.4 122.1 17.0 26 W HOH OH2 1009 183.4 140.4 23.9 19 W HOH OH2 1010 207.0 125.9 37.1 32 W HOH OH2 1011 206.7 121.1 35.1 19 W HOH OH2 1012 205.4 118.4 25.5 19 W HOH OH2 1013 185.7 136.5 27.0 20 W HOH OH2 1014 199.9 116.3 20.3 25 W HOH OH2 1015 182.0 129.2 15.7 24 W HOH OH2 1016 186.1 132.2 24.9 20 W HOH OH2 1017 203.7 128.9 36.9 47 W HOH OH2 1018 190.9 131.9 25.5 20 W HOH OH2 1019 193.8 145.4 6.5 35 W HOH OH2 1020 204.7 110.3 24.0 26 W HOH OH2 1021 190.7 121.4 14.3 36 W HOH OH2 1022 189.0 132.2 33.9 26 W HOH OH2 1023 202.7 108.8 26.0 37 W HOH OH2 1024 186.0 133.7 27.2 25 W HOH OH2 1025 203.0 111.2 38.8 33 W HOH OH2 1026 177.9 139.1 26.5 25 W HOH OH2 1027 209.0 135.8 17.2 38 W HOH OH2 1028 192.1 141.0 25.0 26 W HOH OH2 1029 188.3 132.6 28.9 21 W HOH OH2 1030 195.3 123.1 25.0 33 W HOH OH2 1031 202.0 99.5 32.0 52 W HOH OH2 1032 178.2 161.7 22.7 55 W HOH OH2 1033 179.8 112.9 46.4 55 W HOH OH2 1034 193.3 99.3 34.7 24 W HOH OH2 1035 203.2 106.6 18.6 59 W HOH OH2 1036 206.0 119.0 41.7 31 W HOH OH2 1037 194.1 143.5 18.5 41 W HOH OH2 1038 181.0 141.1 43.3 36 W HOH OH2 1039 207.5 125.2 39.8 31 W HOH OH2 1040 211.7 126.1 33.2 26 W HOH OH2 1041 201.2 127.4 34.1 55 W HOH OH2 1042 202.2 126.6 38.1 42 W HOH OH2 1043 201.8 116.1 34.8 21 W HOH OH2 1044 214.1 122.8 16.0 38 W HOH OH2 1045 213.4 125.5 17.1 41 W HOH OH2 1046 189.0 134.2 35.5 33 W HOH OH2 1047 210.3 117.3 41.7 37 W HOH OH2 1048 193.1 123.1 22.6 36 W HOH OH2 1049 190.1 138.1 27.3 29 W HOH OH2 1050 193.6 126.4 20.8 28 W HOH OH2 1051 209.4 135.7 31.8 65 W HOH OH2 1052 196.9 122.4 17.3 30 W HOH OH2 1053 201.5 108.1 44.1 35 W HOH OH2 1054 187.1 128.5 21.1 27 W HOH OH2 1055 205.6 113.4 35.0 28 W HOH OH2 1056 193.3 138.0 30.0 54 W HOH OH2 1057 168.3 139.7 39.2 41 W HOH OH2 1058 172.8 155.7 11.8 41 W HOH OH2 1059 214.6 89.0 34.3 48 W HOH OH2 1060 178.8 142.9 49.1 50 W HOH OH2 1061 198.5 112.4 25.7 27 W HOH OH2 1062 217.0 94.7 49.2 59 W HOH OH2 1063 189.2 113.4 12.5 51 W HOH OH2 1064 188.9 139.7 36.7 44 W HOH OH2 1065 176.8 142.5 30.0 30 W HOH OH2 1066 195.7 140.7 5.7 26 W HOH OH2 1067 208.4 121.0 41.7 37 W HOH OH2 1068 179.0 145.6 24.4 34 W HOH OH2 1069 197.8 124.7 21.0 28 W HOH OH2 1070 187.5 127.5 24.0 21 W HOH OH2 1071 202.7 132.1 28.7 27 W HOH OH2 1072 198.3 129.7 35.9 36 W HOH OH2 1073 186.4 160.2 7.7 56 W HOH OH2 1074 190.6 115.5 16.4 39 W HOH OH2 1075 174.5 109.8 39.4 51 W HOH OH2 1076 200.6 104.3 31.8 41 W HOH OH2 1077 191.9 134.0 27.1 42 W HOH OH2 1078 189.6 107.5 46.3 32 W HOH OH2 1079 192.4 103.8 21.2 42 W HOH OH2 1080 182.4 122.3 36.5 29 W HOH OH2 1081 188.2 130.9 31.1 31 W HOH OH2 1082 207.2 103.7 26.6 36 W HOH OH2 1083 204.8 133.1 27.2 37 W HOH OH2 1084 214.0 126.7 29.6 29 W HOH OH2 1085 194.6 122.8 45.5 43 W HOH OH2 1086 198.3 108.5 19.3 52 W HOH OH2 1087 203.6 125.2 44.6 21 W HOH OH2 1088 195.8 141.0 8.5 35 W HOH OH2 1089 186.5 150.2 37.0 64 W HOH OH2 1090 203.2 138.6 27.6 62 W HOH OH2 1091 206.1 128.0 33.8 48 W HOH OH2 1092 218.2 128.9 36.9 61 W HOH OH2 1093 188.3 110.9 60.4 76 W HOH OH2 1094 174.2 131.4 16.3 43 W HOH OH2 1095 186.1 139.1 40.9 34 W HOH OH2 1096 171.6 110.3 38.2 54 W HOH OH2 1097 201.1 134.0 30.1 48 W HOH OH2 1098 173.9 123.1 14.6 38 W HOH OH2 1099 203.2 112.0 25.5 34 W HOH OH2 1100 209.2 127.4 33.4 42 W HOH OH2 1101 183.6 103.7 21.0 44 W HOH OH2 1102 194.1 134.0 39.6 31 W HOH OH2 1103 206.5 123.1 41.5 35 W HOH OH2 1104 212.8 134.7 16.5 49 W HOH OH2 1105 215.0 130.6 21.3 41 W HOH OH2 1106 183.4 141.7 41.0 43 W HOH OH2 1107 203.0 116.0 53.9 30 W HOH OH2 1108 197.1 125.1 18.1 35 W HOH OH2 1109 195.9 119.6 10.2 36 W HOH OH2 1110 197.7 127.3 −0.2 43 W HOH OH2 1111 206.4 131.4 42.7 33 W HOH OH2 1112 163.5 127.2 24.4 51 W HOH OH2 1113 196.5 143.6 9.4 54 W HOH OH2 1114 188.8 128.8 18.2 25 W HOH OH2 1115 202.5 103.3 39.3 70 W HOH OH2 1116 202.5 127.7 31.4 41 W HOH OH2 1117 196.3 120.1 19.2 41 W HOH OH2 1118 185.3 130.9 30.7 39 W HOH OH2 1119 193.6 119.5 18.4 45 W HOH OH2 1120 181.9 134.9 21.2 42 W HOH OH2 1121 192.8 101.8 25.5 60 W HOH OH2 1122 188.4 149.2 27.6 63 W HOH OH2 1123 220.5 117.5 28.3 64 W HOH OH2 1124 187.0 131.2 16.7 36 W HOH OH2 1125 212.6 128.7 27.8 36 W HOH OH2 1126 172.3 122.7 12.5 52 W HOH OH2 1127 192.9 133.2 41.8 23 W HOH OH2 1128 189.2 150.4 12.3 60 W HOH OH2 1129 165.9 130.2 23.5 53 W HOH OH2 1130 191.0 132.6 36.8 38 W HOH OH2 1131 172.0 141.0 21.7 49 W HOH OH2 1132 216.5 127.0 35.0 40 W HOH OH2 1133 204.7 101.1 37.6 54 W HOH OH2 1134 205.2 135.8 10.8 53 W HOH OH2 1135 182.9 105.9 23.3 43 W HOH OH2 1136 192.8 135.4 2.0 36 W HOH OH2 1137 169.9 124.1 22.1 35 W HOH OH2 1138 194.9 103.6 27.6 57 W HOH OH2 1139 193.8 147.5 10.8 53 W HOH OH2 1140 175.0 124.9 56.2 55 W HOH OH2 1141 175.6 146.8 25.5 50 W HOH OH2 1142 198.9 144.5 17.4 56 W HOH OH2 1143 176.4 119.9 31.9 43 W HOH OH2 1144 204.6 113.4 44.0 53 W HOH OH2 1145 184.2 100.6 31.8 48 W HOH OH2 1146 215.1 118.7 43.6 24 W HOH OH2 1147 203.6 116.3 46.7 40 W HOH OH2 1148 167.9 119.4 38.0 32 W HOH OH2 1149 199.1 124.3 35.8 46 W HOH OH2 1150 213.7 90.9 37.9 46 W HOH OH2 1151 194.9 128.5 29.0 40 W HOH OH2 1152 189.5 135.1 29.3 47 W HOH OH2 1153 205.0 133.8 13.0 36 W HOH OH2 1154 203.0 109.0 22.1 57 W HOH OH2 1155 176.2 147.6 5.4 53 W HOH OH2 1156 183.7 123.1 11.6 49 W HOH OH2 1157 164.3 135.4 26.2 45 W HOH OH2 1158 192.1 146.7 25.8 55 W HOH OH2 1159 188.8 137.1 36.1 45 W HOH OH2 1160 168.6 109.3 38.1 52 W HOH OH2 1161 205.0 129.0 9.2 28 W HOH OH2 1162 213.2 124.2 30.3 32 W HOH OH2 1163 185.7 122.1 56.4 33 W HOH OH2 1164 206.4 139.7 24.1 62 W HOH OH2 1165 214.0 128.2 25.6 41 W HOH OH2 1166 173.6 145.4 28.5 54 W HOH OH2 1167 163.7 129.1 41.6 44 W HOH OH2 1168 175.7 141.9 48.5 72 W HOH OH2 1169 187.5 123.0 13.4 44 W HOH OH2 1170 185.2 142.8 39.4 63 W HOH OH2 1171 211.2 114.1 9.6 52 W HOH OH2 1172 201.7 110.9 19.4 58 W HOH OH2 1173 206.6 119.5 5.6 48 W HOH OH2 1174 213.9 111.4 12.7 60 W HOH OH2 1175 184.1 119.6 10.4 64 W HOH OH2 1176 213.8 127.8 32.1 38 W HOH OH2 1177 209.4 125.7 11.5 48 W HOH OH2 1178 206.0 109.5 46.6 61 W HOH OH2 1179 201.2 131.8 37.5 90 W HOH OH2 1180 192.5 136.9 26.2 69 W HOH OH2 1181 218.0 119.6 49.4 67 W HOH OH2 1182 176.4 102.9 16.1 68 W HOH OH2 1183 173.6 140.7 17.1 67 W HOH OH2 1184 189.8 116.1 13.4 60 W HOH OH2 1185 181.9 136.3 0.1 92 W HOH OH2 1186 167.2 136.3 31.9 37 W HOH OH2 1187 162.5 114.2 22.1 49 W HOH OH2 1188 196.4 109.8 48.5 42 W HOH OH2 1189 212.8 120.4 15.5 39 W HOH OH2 1190 191.0 102.6 23.4 50 W HOH OH2 1191 196.4 141.1 45.8 56 W HOH OH2 1192 204.0 108.8 40.4 77 W HOH OH2 1193 193.1 143.8 10.7 46 W HOH OH2 1194 207.6 120.3 49.0 57 W HOH OH2 1195 190.8 106.9 18.7 55 W HOH OH2 1196 194.3 126.0 35.2 45 W HOH OH2 1197 161.7 128.1 30.0 35 W HOH OH2 1198 204.3 124.3 60.4 54 W HOH OH2 1199 163.7 107.4 23.3 49 W HOH OH2 1200 215.5 108.1 19.5 34 W HOH OH2 1201 164.4 143.9 24.4 59 W HOH OH2 1202 188.5 149.1 30.8 65 W HOH OH2 1203 192.2 141.0 28.2 61 W HOH OH2 1204 184.8 103.8 15.9 63 W HOH OH2 1205 197.7 114.2 18.5 67 W HOH OH2 1206 219.5 112.6 23.4 60 W HOH OH2 1207 210.2 138.0 22.1 58 W HOH OH2 1208 216.3 128.9 32.8 50 W HOH OH2 1209 186.2 134.3 37.1 47 W HOH OH2 1210 195.7 144.3 4.7 59 W HOH OH2 1211 180.3 104.4 34.4 62 W HOH OH2 1212 165.3 121.4 43.1 62 W HOH OH2 1213 195.6 137.0 40.0 46 W HOH OH2 1214 196.9 112.1 47.4 54 W HOH OH2 1215 220.4 116.7 31.0 75 W HOH OH2 1216 181.5 128.7 58.4 40 W HOH OH2 1217 180.2 142.6 41.3 49 W HOH OH2 1218 200.6 110.1 24.4 39 W HOH OH2 1219 176.3 153.6 20.3 58 W HOH OH2 1220 179.4 142.4 24.9 45 W HOH OH2 1221 179.6 133.8 57.6 57 W HOH OH2 1222 192.3 149.2 13.6 40 W HOH OH2 1223 204.6 123.8 65.8 54 W HOH OH2 1224 195.9 132.1 38.7 42 W HOH OH2 1225 197.4 139.1 40.7 58 W HOH OH2 1226 199.8 123.6 38.6 36 W HOH OH2 1227 215.3 112.9 39.2 44 W HOH OH2 1228 176.6 107.3 21.6 45 W HOH OH2 1229 210.1 129.6 31.6 43 W HOH OH2 1230 190.7 144.2 1.5 81 W HOH OH2 1231 205.1 108.5 13.9 70 W HOH OH2 1232 205.7 136.4 7.1 73 W HOH OH2 1233 189.5 141.8 28.2 70 W HOH OH2 1234 179.7 145.5 41.4 56 W HOH OH2 1235 192.4 132.0 53.2 63 W HOH OH2 1236 214.4 110.1 18.2 41 W HOH OH2 1237 207.6 131.5 5.1 66 W HOH OH2 1238 180.4 127.4 16.8 43 W HOH OH2 1239 201.9 142.7 8.5 93 W HOH OH2 1240 176.1 137.1 9.7 56 W HOH OH2 1241 169.1 111.6 31.5 45 W HOH OH2 1242 181.9 141.6 47.9 66 W HOH OH2 1243 203.1 106.0 34.8 61 W HOH OH2 1244 183.4 102.5 18.1 67 W HOH OH2 1245 191.6 159.6 22.3 31 W HOH OH2 1246 199.3 120.5 54.1 51 W HOH OH2 1247 214.5 112.6 51.3 72 W HOH OH2 1248 205.0 112.7 11.6 40 W HOH OH2 1249 195.7 142.0 22.5 56 W HOH OH2 1250 162.7 131.3 30.6 61 W HOH OH2 1251 173.0 152.1 20.0 59 W HOH OH2 1252 181.5 121.4 11.9 63 W HOH OH2 1253 186.6 115.3 22.2 44 W HOH OH2 1254 182.7 149.4 35.4 74 W HOH OH2 1255 162.9 129.2 38.0 60 W HOH OH2 1256 203.7 141.7 25.4 66 W HOH OH2 1257 212.6 118.9 42.3 40 W HOH OH2 1258 179.7 144.8 45.6 67 W HOH OH2 1259 198.8 108.3 22.4 87 W HOH OH2 1260 196.9 142.5 25.8 62 W HOH OH2 1261 212.8 130.7 30.8 52 W HOH OH2 1262 214.3 93.0 39.5 54 W HOH OH2 1263 178.4 153.2 22.4 67 W HOH OH2 1264 204.7 135.9 25.3 46 W HOH OH2 1265 212.6 117.4 9.9 60 W HOH OH2 1266 179.6 100.0 28.4 67 W HOH OH2 1267 219.8 115.1 20.1 65 W HOH OH2 1268 158.1 126.2 30.7 59 W HOH OH2 1269 171.9 134.2 54.2 60 W HOH OH2 1270 184.0 106.3 37.7 58 W HOH OH2 1271 173.8 118.6 46.9 49 W HOH OH2 1272 215.9 126.1 44.5 41 W HOH OH2 1273 212.1 135.4 24.2 56 W HOH OH2 1274 181.4 140.5 50.8 55 W HOH OH2 1275 210.9 115.0 48.8 59 W HOH OH2 1276 189.9 152.6 15.8 38 W HOH OH2 1277 195.5 129.7 32.0 47 W HOH OH2 1278 181.3 134.6 11.0 72 W HOH OH2 1279 199.4 154.9 21.0 84 W HOH OH2 1280 202.8 101.8 44.1 59 W HOH OH2 1281 190.8 99.5 33.5 60 W HOH OH2 1282 203.1 141.8 21.0 57 W HOH OH2 1283 211.2 117.6 47.8 54 W HOH OH2 1284 203.8 113.8 51.8 56 W GLY C 0 194.2 132.2 35.3 45 P GLY O 0 195.2 131.9 34.7 46 P GLY CA 0 194.0 133.5 36.2 46 P CYS N 1 193.1 131.4 35.4 42 P CYS CA 1 193.1 130.2 34.6 39 P CYS CB 1 192.8 129.1 35.6 40 P CYS SG 1 194.0 129.0 36.9 40 P CYS C 1 192.1 130.3 33.5 38 P CYS O 1 190.9 130.5 33.8 38 P VAL N 2 192.6 130.3 32.3 36 P VAL CA 2 191.7 130.4 31.1 35 P VAL CB 2 192.5 131.0 29.9 35 P VAL CG1 2 191.7 131.1 28.7 35 P VAL CG2 2 193.0 132.4 30.3 36 P VAL C 2 191.3 129.0 30.7 34 P VAL O 2 192.1 128.1 30.3 35 P ILE N 3 190.0 128.7 30.9 32 P ILE CA 3 189.4 127.4 30.6 29 P ILE CB 3 188.5 126.8 31.7 27 P ILE CG2 3 189.4 126.6 33.0 24 P ILE CG1 3 187.3 127.6 32.0 25 P ILE CD1 3 186.4 127.0 33.0 23 P ILE C 3 188.7 127.3 29.2 28 P ILE O 3 188.2 126.2 28.8 26 P MET N 4 188.5 128.4 28.5 28 P MET CA 4 188.0 128.5 27.2 29 P MET CB 4 186.5 128.0 27.1 31 P MET CG 4 185.4 128.8 26.3 34 P MET CE 4 183.3 130.4 25.9 33 P MET SD 4 184.2 129.9 27.3 36 P MET C 4 188.3 129.8 26.4 31 P MET OT1 4 188.0 129.8 25.2 32 P MET OT2 4 189.0 130.7 26.9 30 P

TABLE 3 The following table lists the atomic structure coordinates for FPT in complex with FPP and the inhibitor SCH66381 as derived by X-ray diffraction from crystals of that complex. The abbreviations are the same as those used in Table 2. RES ATOM # X Y Z B C GLY C 54 192.3 151.6 9.2 83 A GLY O 54 191.1 151.5 9.3 83 A GLY N 54 193.3 151.1 7.0 84 A GLY CA 54 192.9 152.2 7.9 83 A PHE N 55 193.2 151.2 10.1 82 A PHE CA 55 192.8 150.6 11.4 81 A PHE CB 55 193.7 149.4 11.7 81 A PHE CG 55 193.1 148.1 11.2 82 A PHE CD1 55 193.7 147.4 10.1 82 A PHE CD2 55 192.1 147.4 11.9 81 A PHE CE1 55 193.2 146.2 9.7 82 A PHE CE2 55 191.6 146.2 11.5 82 A PHE CZ 55 192.2 145.6 10.4 82 A PHE C 55 192.8 151.6 12.5 79 A PHE O 55 193.8 152.4 12.6 79 A LEU N 56 191.8 151.7 13.3 76 A LEU CA 56 191.7 152.6 14.4 73 A LEU CB 56 190.5 153.4 14.5 72 A LEU CG 56 190.6 154.9 14.7 72 A LEU CD1 56 189.3 155.5 15.1 72 A LEU CD2 56 191.7 155.2 15.8 72 A LEU C 56 191.9 151.7 15.7 70 A LEU O 56 190.9 151.2 16.2 70 A SER N 57 193.1 151.6 16.2 66 A SER CA 57 193.4 150.8 17.4 63 A SER CB 57 194.9 151.0 17.8 64 A SER OG 57 195.2 150.3 19.0 64 A SER C 57 192.5 151.1 18.6 61 A SER O 57 192.2 152.2 18.9 60 A LEU N 58 192.0 150.0 19.2 59 A LEU CA 58 191.2 150.1 20.4 57 A LEU CB 58 190.9 148.7 20.9 55 A LEU CG 58 189.4 148.2 20.8 54 A LEU CD1 58 189.3 146.8 21.4 54 A LEU CD2 58 188.5 149.2 21.6 53 A LEU C 58 191.8 150.9 21.5 57 A LEU O 58 191.2 151.4 22.4 57 A ASP N 59 193.2 150.9 21.5 56 A ASP CA 59 194.0 151.7 22.4 56 A ASP CB 59 195.2 150.9 22.8 59 A ASP CG 59 195.1 150.1 24.1 62 A ASP OD1 59 194.5 149.0 24.0 63 A ASP OD2 59 195.7 150.6 25.1 63 A ASP C 59 194.4 153.1 22.0 52 A ASP O 59 194.9 153.9 22.9 51 A SER N 60 194.2 153.4 20.8 49 A SER CA 60 194.5 154.7 20.2 46 A SER CB 60 194.0 154.7 18.8 46 A SER OG 60 194.1 156.0 18.2 47 A SER C 60 193.9 155.8 21.0 45 A SER O 60 192.8 155.7 21.4 45 A PRO N 61 194.7 156.9 21.2 43 A PRO CD 61 196.1 157.2 20.8 43 A PRO CA 61 194.2 158.0 22.0 42 A PRO CB 61 195.4 158.9 22.2 42 A PRO CG 61 196.2 158.7 20.9 42 A PRO C 61 193.0 158.7 21.3 41 A PRO O 61 192.1 159.3 21.9 41 A THR N 62 193.0 158.5 19.9 40 A THR CA 62 192.0 159.1 19.1 40 A THR CB 62 192.6 159.9 17.9 40 A THR OG1 62 193.4 159.0 17.1 40 A THR CG2 62 193.6 161.0 18.4 40 A THR C 62 191.0 158.1 18.6 40 A THR O 62 190.3 158.4 17.6 42 A TYR N 63 190.8 157.0 19.3 39 A TYR CA 63 189.8 156.0 18.9 37 A TYR CB 63 190.0 154.7 19.7 37 A TYR CG 63 188.9 153.7 19.6 36 A TYR CD1 63 188.9 152.7 18.5 36 A TYR CE1 63 187.9 151.8 18.4 35 A TYR CD2 63 187.8 153.7 20.5 36 A TYR CE2 63 186.8 152.7 20.3 35 A TYR CZ 63 186.8 151.8 19.3 35 A TYR OH 63 185.8 150.9 19.2 34 A TYR C 63 188.5 156.6 19.2 36 A TYR O 63 188.3 157.3 20.1 36 A VAL N 64 187.5 156.4 18.3 36 A VAL CA 64 186.2 156.9 18.5 35 A VAL CB 64 185.8 158.0 17.4 35 A VAL CG1 64 186.7 159.3 17.6 34 A VAL CG2 64 186.0 157.5 16.0 35 A VAL C 64 185.1 155.8 18.4 36 A VAL O 64 185.3 154.8 17.6 37 A LEU N 65 184.1 155.9 19.2 35 A LEU CA 65 183.0 154.9 19.2 34 A LEU CB 65 181.9 155.3 20.2 31 A LEU CG 65 182.4 155.4 21.6 30 A LEU CD1 65 181.2 155.8 22.5 31 A LEU CD2 65 182.9 154.1 22.2 30 A LEU C 65 182.4 154.7 17.8 36 A LEU O 65 182.4 155.7 17.1 37 A TYR N 66 182.0 153.6 17.5 38 A TYR CA 66 181.4 153.3 16.2 39 A TYR CB 66 181.0 151.8 16.0 38 A TYR CG 66 182.2 150.9 15.7 37 A TYR CD1 66 183.0 150.5 16.7 36 A TYR CE1 66 184.1 149.8 16.3 36 A TYR CD2 66 182.4 150.6 14.3 36 A TYR CE2 66 183.6 149.9 14.0 35 A TYR CZ 66 184.4 149.5 15.0 35 A TYR OH 66 185.6 148.8 14.7 35 A TYR C 66 180.2 154.2 15.8 40 A TYR O 66 179.9 154.5 14.7 40 A ARG N 67 179.5 154.6 16.9 41 A ARG CA 67 178.3 155.4 16.7 43 A ARG CB 67 177.4 155.4 17.9 44 A ARG CG 67 178.0 155.9 19.2 45 A ARG CD 67 176.9 156.1 20.3 46 A ARG NE 67 177.4 156.6 21.5 47 A ARG CZ 67 177.6 155.9 22.6 48 A ARG NH1 67 177.3 154.6 22.7 49 A ARG NH2 67 178.0 156.5 23.7 49 A ARG C 67 178.7 156.9 16.4 44 A ARG O 67 177.8 T57.7 16.1 45 A ASP N 68 179.9 157.2 16.5 44 A ASP CA 68 180.4 158.6 16.2 43 A ASP CB 68 181.3 159.1 17.3 42 A ASP CG 68 180.6 159.4 18.6 42 A ASP OD1 68 179.3 159.7 18.6 42 A ASP OD2 68 181.2 159.3 19.7 41 A ASP C 68 181.1 158.5 14.9 44 A ASP O 68 181.8 159.4 14.5 45 A ARG N 69 181.0 157.4 14.2 45 A ARG CA 69 181.7 157.1 12.9 47 A ARG CB 69 182.4 155.8 12.9 46 A ARG CG 69 183.3 155.5 14.1 45 A ARG CD 69 184.3 154.4 13.8 44 A ARG NE 69 185.1 153.9 15.0 42 A ARG CZ 69 186.1 153.1 14.9 41 A ARG NH1 69 186.5 152.6 13.8 40 A ARG NH2 69 186.7 152.7 16.0 41 A ARG C 69 180.8 157.3 11.7 48 A ARG O 69 179.8 156.6 11.5 49 A ALA N 70 181.3 158.2 10.8 51 A ALA CA 70 180.6 158.5 9.5 52 A ALA CB 70 181.3 159.7 8.8 53 A ALA C 70 180.4 157.4 8.6 53 A ALA O 70 179.4 157.3 7.9 54 A GLU N 71 181.3 156.5 8.5 53 A GLU CA 71 181.3 155.3 7.6 54 A GLU CB 71 182.7 154.9 7.2 55 A GLU CG 71 183.6 154.3 8.4 56 A GLU CD 71 183.9 155.3 9.5 56 A GLU OE1 71 184.0 154.9 10.7 56 A GLU OE2 71 184.0 156.5 9.2 57 A GLU C 71 180.5 154.2 8.3 53 A GLU O 71 180.5 153.0 7.7 53 A TRP N 72 179.9 154.4 9.4 54 A TRP CA 72 179.1 153.5 10.2 55 A TRP CB 72 179.9 153.1 11.5 54 A TRP CG 72 180.9 152.0 11.3 52 A TRP CD2 72 180.7 150.6 11.1 51 A TRP CE2 72 181.9 150.0 10.8 51 A TRP CE3 72 179.5 149.8 11.0 51 A TRP CD1 72 182.2 152.2 11.2 52 A TRP NE1 72 182.9 151.0 10.9 52 A TRP CZ2 72 182.0 148.6 10.6 51 A TRP CZ3 72 179.6 148.5 10.8 51 A TRP CH2 72 180.9 147.9 10.6 51 A TRP C 72 177.7 154.0 10.6 58 A TRP O 72 176.9 153.2 11.2 58 A ALA N 73 177.4 155.2 10.3 60 A ALA CA 73 176.1 155.8 10.6 61 A ALA CB 73 176.2 157.3 10.5 61 A ALA C 73 175.0 155.2 9.8 62 A ALA O 73 173.8 155.2 10.2 63 A ASP N 74 175.3 154.7 8.6 61 A ASP CA 74 174.3 154.1 7.7 61 A ASP CB 74 174.9 153.8 6.4 61 A ASP CG 74 175.9 152.7 6.4 61 A ASP OD1 74 175.6 151.6 5.8 62 A ASP OD2 74 176.9 152.8 7.1 61 A ASP C 74 173.7 152.8 8.3 61 A ASP O 74 172.5 152.4 8.0 61 A ILE N 75 174.4 152.1 9.2 60 A ILE CA 75 174.0 150.9 9.8 59 A ILE CB 75 175.1 149.8 9.8 58 A ILE CG2 75 175.9 149.9 11.1 58 A ILE CG1 75 174.5 148.4 9.7 58 A ILE CD1 75 175.5 147.3 9.7 58 A ILE C 75 173.4 151.1 11.2 58 A ILE O 75 173.9 152.0 12.0 59 A ASP N 76 172.4 150.4 11.6 58 A ASP CA 76 171.7 150.5 12.8 58 A ASP CB 76 170.2 150.2 12.7 60 A ASP CG 76 169.3 151.4 12.8 62 A ASP OD1 76 169.3 152.3 11.9 63 A ASP OD2 76 168.6 151.5 13.9 63 A ASP C 76 172.2 149.5 13.9 56 A ASP O 76 172.1 148.3 13.6 55 A PRO N 77 172.8 149.9 15.0 54 A PRO CD 77 173.1 151.3 15.3 54 A PRO CA 77 173.3 149.0 16.0 53 A PRO CB 77 174.0 149.9 17.0 53 A PRO CG 77 173.3 151.2 16.8 54 A PRO C 77 172.2 148.2 16.7 52 A PRO O 77 171.1 148.7 16.9 51 A VAL N 78 172.5 147.0 17.0 51 A VAL CA 78 171.5 146.1 17.6 49 A VAL CB 78 171.4 144.7 16.8 49 A VAL CG1 78 170.5 143.8 17.5 49 A VAL CG2 78 171.1 145.0 15.4 49 A VAL C 78 172.0 145.8 19.0 50 A VAL O 78 173.0 145.1 19.2 50 A PRO N 79 171.3 146.3 20.0 50 A PRO CD 79 170.3 147.3 19.9 50 A PRO CA 79 171.7 146.1 21.4 50 A PRO CB 79 170.8 147.2 22.2 50 A PRO CG 79 169.6 147.3 21.3 50 A PRO C 79 171.4 144.7 21.9 50 A PRO O 79 170.5 144.0 21.4 50 A GLN N 80 172.1 144.2 22.9 49 A GLN CA 80 171.9 142.9 23.4 49 A GLN CB 80 173.1 142.5 24.4 48 A GLN CG 80 173.0 141.1 24.9 45 A GLN CD 80 174.3 140.6 25.5 45 A GLN OE1 80 175.1 139.9 24.9 45 A GLN NE2 80 174.4 140.9 26.8 45 A GLN C 80 170.6 142.8 24.1 50 A GLN O 80 170.2 143.6 24.9 51 A ASN N 81 169.9 141.7 23.9 51 A ASN CA 81 168.7 141.4 24.5 50 A ASN CB 81 167.7 140.9 23.4 51 A ASN CG 81 166.3 140.5 24.0 52 A ASN OD1 81 166.0 140.9 25.1 52 A ASN ND2 81 165.6 139.7 23.2 53 A ASN C 81 168.8 140.3 25.6 50 A ASN O 81 168.9 139.1 25.3 50 A ASP N 82 168.9 140.8 26.8 51 A ASP CA 82 169.1 139.9 28.0 52 A ASP CB 82 170.0 140.6 29.0 53 A ASP CG 82 171.5 140.5 28.6 54 A ASP OD1 82 171.8 139.6 27.8 53 A ASP OD2 82 172.3 141.2 29.3 54 A ASP C 82 167.7 139.7 28.6 53 A ASP O 82 167.7 139.1 29.7 53 A GLY N 83 166.7 140.2 28.0 53 A GLY CA 83 165.3 140.1 28.5 55 A GLY C 83 165.0 141.1 29.6 56 A GLY O 83 165.9 141.7 30.2 57 A PRO N 84 163.7 141.3 29.8 56 A PRO CD 84 162.6 140.5 29.2 55 A PRO CA 84 163.2 142.3 30.8 55 A PRO CB 84 161.7 142.0 30.8 56 A PRO CG 84 161.6 140.6 30.4 56 A PRO C 84 163.8 142.1 32.2 55 A PRO O 84 163.8 143.1 32.9 55 A SER N 85 164.2 140.9 32.5 54 A SER CA 85 164.8 140.7 33.8 53 A SER CB 85 163.8 139.9 34.7 54 A SER OG 85 162.5 140.6 34.8 55 A SER C 85 166.0 139.9 33.7 53 A SER O 85 166.0 138.7 33.9 53 A PRO N 86 167.2 140.6 33.5 51 A PRO CD 86 167.2 142.0 33.2 51 A PRO CA 86 168.5 140.0 33.4 50 A PRO CB 86 169.4 141.2 33.1 50 A PRO CG 86 168.5 142.1 32.3 50 A PRO C 86 169.0 139.2 34.6 48 A PRO O 86 168.6 139.4 35.7 48 A VAL N 87 169.9 138.3 34.3 45 A VAL CA 87 170.6 137.5 35.3 41 A VAL CB 87 170.1 136.0 35.4 41 A VAL CG1 87 168.9 136.0 36.4 41 A VAL CG2 87 169.6 135.5 34.1 41 A VAL C 87 172.1 137.5 34.8 39 A VAL O 87 172.3 137.7 33.6 38 A VAL N 88 173.0 137.3 35.7 36 A VAL CA 88 174.4 137.3 35.4 35 A VAL CB 88 175.0 135.9 35.1 34 A VAL CG1 88 174.9 135.0 36.3 33 A VAL CG2 88 174.4 135.3 33.9 33 A VAL C 88 174.7 138.3 34.3 36 A VAL O 88 175.3 138.0 33.3 37 A GLN N 89 174.2 139.5 34.5 36 A GLN CA 89 174.3 140.6 33.6 36 A GLN CB 89 173.1 141.6 33.8 36 A GLN CG 89 173.2 142.8 33.0 38 A GLN CD 89 172.1 143.8 33.3 38 A GLN OE1 89 171.8 144.1 34.4 38 A GLN NE2 89 171.5 144.2 32.2 38 A GLN C 89 175.6 141.4 33.7 37 A GLN O 89 176.0 141.8 34.8 37 A ILE N 90 176.3 141.6 32.6 35 A ILE CA 90 177.6 142.2 32.7 35 A ILE CB 90 178.5 141.6 31.7 34 A ILE CG2 90 179.9 142.2 31.8 34 A ILE CG1 90 178.6 140.0 31.9 33 A ILE CD1 90 179.2 139.2 30.8 32 A ILE C 90 177.5 143.7 32.3 35 A ILE O 90 177.0 144.1 31.2 36 A ILE N 91 177.9 144.5 33.3 36 A ILE CA 91 177.8 146.0 33.1 37 A ILE CB 91 177.9 146.7 34.4 37 A ILE CG2 91 177.9 148.3 34.2 38 A ILE CG1 91 176.8 146.3 35.4 37 A ILE CD1 91 175.4 146.6 34.8 38 A ILE C 91 178.9 146.4 32.1 36 A ILE O 91 180.0 146.9 32.5 36 A TYR N 92 178.7 146.2 30.8 36 A TYR CA 92 179.7 146.5 29.8 38 A TYR CB 92 179.2 146.2 28.4 37 A TYR CG 92 178.6 144.8 28.2 37 A TYR CD1 92 177.4 144.7 27.7 37 A TYR CE1 92 176.8 143.4 27.6 37 A TYR CD2 92 179.3 143.7 28.6 37 A TYR CE2 92 178.8 142.4 28.5 37 A TYR CZ 92 177.5 142.3 28.0 36 A TYR OH 92 176.8 141.1 27.9 36 A TYR C 92 180.1 147.9 29.9 39 A TYR O 92 179.3 148.8 30.2 39 A SER N 93 181.3 148.2 29.5 40 A SER CA 93 181.9 149.5 29.4 41 A SER CB 93 163.4 149.5 29.2 42 A SER OG 93 183.7 148.8 28.0 43 A SER C 93 181.2 150.0 28.1 42 A SER O 93 180.5 149.3 27.4 42 A GLU N 94 181.4 151.3 27.7 43 A GLU CA 94 180.8 151.9 26.5 44 A GLU CB 94 180.8 153.4 26.6 47 A GLU CG 94 180.0 154.0 25.5 50 A GLU CD 94 179.0 154.9 26.2 53 A GLU OE1 94 178.0 154.5 26.8 53 A GLU OE2 94 179.3 156.2 26.1 54 A GLU C 94 181.4 151.4 25.2 42 A GLU O 94 180.7 151.3 24.2 41 A LYS N 95 182.7 151.3 25.2 42 A LYS CA 95 183.4 150.9 24.0 41 A LYS CB 95 185.0 150.9 24.3 41 A LYS CG 95 185.5 152.3 24.7 42 A LYS CD 95 187.0 152.1 25.1 43 A LYS CE 95 187.8 151.4 24.1 43 A LYS NZ 95 189.2 151.0 24.6 43 A LYS C 95 183.0 149.4 23.8 40 A LYS O 95 182.7 149.1 22.6 41 A PHE N 96 183.0 148.6 24.8 39 A PHE CA 96 182.7 147.2 24.7 37 A PHE CB 96 182.7 146.5 26.0 35 A PHE CG 96 182.5 145.0 25.9 34 A PHE CD1 96 183.6 144.1 26.0 34 A PHE CD2 96 181.3 144.5 25.7 34 A PHE CE1 96 183.4 142.7 25.9 33 A PHE CE2 96 181.0 143.1 25.6 32 A PHE CZ 96 182.1 142.2 25.7 33 A PHE C 96 181.2 147.1 24.1 38 A PHE O 96 181.0 146.6 23.0 38 A ARG N 97 180.3 147.7 24.9 40 A ARG CA 97 178.9 147.7 24.5 41 A ARG CB 97 178.1 148.6 25.4 43 A ARG CG 97 176.7 148.2 25.6 47 A ARG CD 97 175.8 149.4 26.0 50 A ARG NE 97 176.3 150.2 27.1 53 A ARG CZ 97 177.0 151.3 26.9 55 A ARG NH1 97 177.3 151.8 25.7 56 A ARG NH2 97 177.5 151.9 28.0 55 A ARG C 97 178.8 148.2 23.0 40 A ARG O 97 178.1 147.6 22.2 41 A ASP N 98 179.4 149.4 22.8 39 A ASP CA 98 179.4 150.0 21.4 38 A ASP CB 98 180.3 151.3 21.5 38 A ASP CG 98 180.5 151.9 20.1 38 A ASP OD1 98 179.6 152.6 19.6 39 A ASP OD2 98 181.5 151.7 19.5 37 A ASP C 98 179.8 149.1 20.3 36 A ASP O 98 179.1 148.9 19.3 36 A VAL N 99 181.0 148.4 20.4 34 A VAL CA 99 181.5 147.5 19.4 32 A VAL CB 99 182.9 147.0 19.7 31 A VAL CG1 99 183.3 145.8 18.8 29 A VAL CG2 99 183.9 148.1 19.5 30 A VAL C 99 180.6 146.3 19.1 32 A VAL O 99 180.3 145.9 18.0 32 A TYR N 100 180.0 145.8 20.2 32 A TYR CA 100 179.2 144.6 20.1 31 A TYR CB 100 179.1 143.9 21.4 29 A TYR CG 100 180.3 142.9 21.5 27 A TYR CD1 100 181.4 143.3 22.1 26 A TYR CE1 100 182.5 142.5 22.1 25 A TYR CD2 100 180.2 141.7 20.8 27 A TYR CE2 100 181.3 140.9 20.8 26 A TYR CZ 100 182.5 141.3 21.4 26 A TYR OH 100 183.5 140.4 21.4 26 A TYR C 100 177.8 145.0 19.5 33 A TYR O 100 177.3 144.2 18.6 36 A ASP N 101 177.2 146.1 19.9 34 A ASP CA 101 175.9 146.5 19.3 34 A ASP CB 101 175.5 147.8 19.8 36 A ASP CG 101 174.9 147.8 21.2 37 A ASP OD1 101 174.8 146.8 21.8 37 A ASP OD2 101 174.5 148.9 21.6 39 A ASP C 101 176.1 146.5 17.8 34 A ASP O 101 175.3 146.1 17.0 35 A TYR N 102 177.3 147.0 17.4 35 A TYR CA 102 177.6 147.1 16.0 36 A TYR CB 102 178.7 148.1 15.7 37 A TYR CG 102 178.1 149.5 15.4 38 A TYR CD1 102 177.8 149.8 14.1 39 A TYR CE1 102 177.2 151.0 13.8 39 A TYR CD2 102 177.9 150.4 16.4 36 A TYR CE2 102 177.2 151.6 16.2 39 A TYR CZ 102 176.9 151.9 14.9 40 A TYR OH 102 176.3 153.1 14.6 40 A TYR C 102 177.9 145.7 15.4 36 A TYR O 102 177.4 145.4 14.2 36 A PHE N 103 178.5 144.8 16.1 36 A PHE CA 103 178.8 143.4 15.6 36 A PHE CB 103 179.7 142.6 16.6 33 A PHE CG 103 179.9 141.1 16.2 32 A PHE CD1 103 180.7 140.8 15.1 32 A PHE CD2 103 179.2 140.1 16.8 31 A PHE CE1 103 180.9 139.5 14.7 30 A PHE CE2 103 179.3 138.8 16.4 29 A PHE CZ 103 180.1 138.4 15.3 29 A PHE C 103 177.4 142.8 15.4 37 A PHE O 103 177.2 142.2 14.3 37 A ARG N 104 176.6 142.8 16.4 39 A ARG CA 104 175.2 142.2 16.3 40 A ARG CB 104 174.3 142.6 17.5 40 A ARG CG 104 174.8 141.9 18.7 41 A ARG CD 104 174.0 142.4 19.9 42 A ARG NE 104 174.6 142.0 21.1 45 A ARG CZ 104 175.4 142.8 21.9 46 A ARG NH1 104 175.6 144.1 21.6 46 A ARG NH2 104 176.0 142.3 23.0 47 A ARG C 104 174.5 142.7 15.0 40 A ARG O 104 173.8 141.9 14.3 40 A ALA N 105 174.7 144.0 14.7 40 A ALA CA 105 174.1 144.5 13.5 41 A ALA CB 105 174.3 146.0 13.4 41 A ALA C 105 174.6 143.9 12.2 41 A ALA O 105 173.8 143.4 11.4 42 A VAL N 106 175.9 143.8 12.1 42 A VAL CA 106 176.6 143.3 10.9 43 A VAL CB 106 178.1 143.6 10.9 43 A VAL CG1 106 178.9 142.6 10.1 44 A VAL CG2 106 178.4 145.0 10.4 43 A VAL C 106 176.4 141.8 10.8 43 A VAL O 106 176.2 141.2 9.7 42 A LEU N 107 176.4 141.1 11.9 43 A LEU CA 107 176.2 139.7 12.0 45 A LEU CB 107 176.4 139.1 13.4 43 A LEU CG 107 176.3 137.6 13.5 42 A LEU CD1 107 177.5 137.1 12.7 42 A LEU CD2 107 176.4 137.1 14.9 41 A LEU C 107 174.8 139.4 11.5 47 A LEU O 107 174.5 138.6 10.6 47 A GLN N 108 173.8 140.1 12.1 51 A GLN CA 108 172.4 139.9 11.8 54 A GLN CB 108 171.6 141.1 12.4 56 A GLN CG 108 170.6 140.8 13.6 59 A GLN CD 108 171.3 140.4 14.9 61 A GLN OE1 108 170.8 140.8 16.0 63 A GLN NE2 108 172.4 139.8 14.8 62 A GLN C 108 172.1 139.9 10.3 54 A GLN O 108 171.5 139.0 9.8 55 A ARG N 109 172.6 140.9 9.6 53 A ARG CA 109 172.5 141.0 8.2 53 A ARG CB 109 172.5 142.5 7.8 55 A ARG CG 109 173.8 143.2 8.1 58 A ARG CD 109 173.7 144.7 7.7 59 A ARG NE 109 172.7 145.4 8.4 62 A ARG CZ 109 171.9 146.3 7.9 63 A ARG NH1 109 172.1 146.7 6.6 64 A ARG NH2 109 171.0 147.0 8.6 63 A ARG C 109 173.5 140.2 7.5 51 A ARG O 109 173.5 140.3 6.2 51 A ASP N 110 174.4 139.6 8.2 49 A ASP CA 110 175.5 138.8 7.5 48 A ASP CB 110 174.9 137.5 6.9 48 A ASP CG 110 176.0 136.6 6.3 48 A ASP OD1 110 177.0 136.5 6.9 48 A ASP OD2 110 175.7 136.1 5.2 48 A ASP C 110 176.1 139.7 6.5 47 A ASP O 110 176.3 139.3 5.3 47 A GLU N 111 176.5 140.8 6.9 47 A GLU CA 111 177.2 141.8 6.1 47 A GLU CB 111 177.1 143.2 6.7 47 A GLU CG 111 177.6 144.3 5.8 47 A GLU CD 111 177.7 145.6 6.6 47 A GLU OE1 111 178.9 146.1 6.7 47 A GLU OE2 111 176.7 146.1 7.1 47 A GLU C 111 178.6 141.3 6.0 47 A GLU O 111 179.4 141.4 6.9 47 A ARG N 112 179.0 140.8 4.8 47 A ARG CA 112 180.4 140.3 4.6 46 A ARG CB 112 180.3 139.0 3.9 46 A ARG CG 112 179.5 138.0 4.6 47 A ARG CD 112 179.4 136.7 3.9 48 A ARG NE 112 178.5 135.8 4.6 48 A ARG CZ 112 178.3 134.5 4.4 49 A ARG NH1 112 179.0 133.9 3.4 49 A ARG NH2 112 177.5 133.8 5.1 49 A ARG C 112 181.2 141.4 4.0 47 A ARG O 112 181.7 141.2 2.9 47 A SER N 113 181.5 142.4 4.7 47 A SER CA 113 182.3 143.5 4.2 46 A SER CB 113 181.5 144.8 4.3 46 A SER OG 113 181.2 145.2 5.7 46 A SER C 113 183.6 143.7 5.0 45 A SER O 113 183.8 143.2 6.1 44 A GLU N 114 184.5 144.5 4.3 44 A GLU CA 114 185.8 144.8 4.8 44 A GLU CB 114 186.5 145.7 3.8 45 A GLU CG 114 187.8 146.2 4.2 47 A GLU CD 114 188.8 145.1 4.4 48 A GLU OE1 114 189.6 145.2 5.4 49 A GLU OE2 114 188.9 144.1 3.7 48 A GLU C 114 185.7 145.6 6.1 43 A GLU O 114 186.5 145.4 7.0 43 A ARG N 115 184.6 146.4 6.3 43 A ARG CA 115 184.4 147.1 7.5 43 A ARG CB 115 183.4 148.3 7.3 43 A ARG CG 115 182.0 147.8 6.9 44 A ARG CD 115 181.1 149.0 6.9 46 A ARG NE 115 179.7 148.7 6.6 48 A ARG CZ 115 178.6 149.4 6.9 48 A ARG NH1 115 177.4 149.0 6.6 49 A ARG NH2 115 178.7 150.5 7.6 49 A ARG C 115 184.0 146.1 8.6 42 A ARG O 115 184.3 146.3 9.7 43 A ALA N 116 183.2 145.1 8.2 40 A ALA CA 116 182.7 144.1 9.1 39 A ALA CB 116 181.7 143.2 8.5 38 A ALA C 116 183.9 143.3 9.6 38 A ALA O 116 184.1 142.9 10.8 37 A PHE N 117 184.9 143.2 8.7 36 A PHE CA 117 186.1 142.5 8.9 35 A PHE CB 117 186.9 142.3 7.6 34 A PHE CG 117 188.2 141.7 7.8 33 A PHE CD1 117 188.3 140.3 8.1 32 A PHE CD2 117 189.4 142.4 7.6 33 A PHE CE1 117 189.6 139.7 8.3 32 A PHE CE2 117 190.6 141.8 7.8 31 A PHE CZ 117 190.7 140.5 8.2 31 A PHE C 117 187.0 143.2 9.9 34 A PHE O 117 187.5 142.6 10.9 34 A LYS N 118 187.1 144.5 9.8 33 A LYS CA 118 187.9 145.3 10.7 33 A LYS CB 118 188.2 146.7 10.2 35 A LYS CG 118 189.1 146.7 8.9 37 A LYS CD 118 189.7 148.1 8.7 39 A LYS CE 118 190.5 148.2 7.4 40 A LYS NZ 118 189.5 148.1 6.2 41 A LYS C 118 187.2 145.4 12.1 31 A LYS O 118 187.9 145.5 13.1 30 A LEU N 119 185.9 145.3 12.1 30 A LEU CA 119 185.2 145.4 13.4 28 A LEU CB 119 183.7 145.7 13.2 27 A LEU CG 119 182.8 145.5 14.4 26 A LEU CD1 119 183.2 146.5 15.5 27 A LEU CD2 119 181.4 145.8 14.0 27 A LEU C 119 185.4 144.1 14.3 28 A LEU O 119 185.3 144.2 15.5 27 A THR N 120 185.5 143.0 13.6 28 A THR CA 120 185.6 141.7 14.3 28 A THR CB 120 185.7 140.5 13.4 27 A THR OG1 120 186.8 140.7 12.4 26 A THR CG2 120 184.4 140.3 12.7 27 A THR C 120 186.9 141.8 15.1 28 A THR O 120 187.0 141.3 16.2 29 A ARG N 121 187.9 142.4 14.5 28 A ARG CA 121 189.2 142.6 15.2 29 A ARG CB 121 190.2 143.3 14.4 31 A ARG CG 121 191.5 143.6 15.2 35 A ARG CD 121 192.3 144.6 14.5 39 A ARG NE 121 193.1 144.0 13.5 43 A ARG CZ 121 194.4 144.2 13.4 45 A ARG NH1 121 195.1 143.6 12.4 45 A ARG NH2 121 195.1 144.9 14.4 45 A ARG C 121 189.1 143.3 16.5 30 A ARG O 121 189.8 143.0 17.5 30 A ASP N 122 188.2 144.3 16.6 28 A ASP CA 122 187.9 145.1 17.8 27 A ASP CB 122 187.2 146.4 17.5 27 A ASP CG 122 188.2 147.5 17.0 28 A ASP OD1 122 189.4 147.4 17.2 28 A ASP OD2 122 187.7 148.5 16.5 30 A ASP C 122 187.1 144.3 18.8 26 A ASP O 122 187.3 144.4 20.0 25 A ALA N 123 186.1 143.5 18.3 26 A ALA CA 123 185.2 142.7 19.1 25 A ALA CB 123 184.1 142.1 18.2 24 A ALA C 123 186.1 141.5 19.7 25 A ALA O 123 185.9 141.2 20.8 27 A ILE N 124 187.0 141.0 18.9 25 A ILE CA 124 187.9 139.9 19.3 25 A ILE CB 124 188.7 139.4 18.2 23 A ILE CG2 124 190.0 138.8 18.7 23 A ILE CG1 124 187.9 138.5 17.3 23 A ILE CD1 124 188.5 138.1 16.0 21 A ILE C 124 188.8 140.5 20.4 26 A ILE O 124 189.0 139.9 21.4 27 A GLU N 125 189.3 141.7 20.1 28 A GLU CA 125 190.2 142.3 21.1 30 A GLU CB 125 190.8 143.6 20.5 34 A GLU CG 125 192.0 144.1 21.1 41 A GLU CD 125 192.7 145.3 20.4 45 A GLU OE1 125 193.6 146.0 21.0 47 A GLU OE2 125 192.3 145.5 19.2 47 A GLU C 125 189.5 142.6 22.4 29 A GLU O 125 190.2 142.6 23.5 29 A LEU N 126 188.2 142.8 22.4 28 A LEU CA 126 187.4 143.1 23.6 25 A LEU CB 126 186.1 143.8 23.2 25 A LEU CG 126 186.3 145.3 22.8 24 A LEU CD1 126 185.0 145.8 22.3 24 A LEU CD2 126 186.7 146.1 24.0 24 A LEU C 126 187.1 141.8 24.4 25 A LEU O 126 187.1 141.8 25.6 26 A ASN N 127 186.9 140.7 23.7 24 A ASN CA 127 186.7 139.4 24.3 23 A ASN CB 127 185.3 139.2 24.7 21 A ASN CG 127 185.0 137.9 25.3 19 A ASN OD1 127 186.0 137.3 25.8 20 A ASN ND2 127 183.8 137.4 25.3 19 A ASN C 127 187.2 138.3 23.4 23 A ASN O 127 186.5 137.8 22.6 24 A ALA N 128 188.5 138.0 23.5 22 A ALA CA 128 189.1 137.0 22.6 22 A ALA CB 128 190.6 137.0 22.9 21 A ALA C 128 188.6 135.6 22.7 23 A ALA O 128 188.9 134.8 21.9 24 A ALA N 129 187.7 135.4 23.7 22 A ALA CA 129 187.1 134.1 23.9 20 A ALA CB 129 187.0 133.8 25.4 19 A ALA C 129 185.8 134.0 23.2 22 A ALA O 129 185.0 133.0 23.4 22 A ASN N 130 185.4 135.0 22.5 21 A ASN CA 130 184.1 135.0 21.9 22 A ASN CB 130 183.6 136.5 21.6 24 A ASN CG 130 182.1 136.5 21.3 25 A ASN OD1 130 181.6 135.7 20.5 27 A ASN ND2 130 181.3 137.4 21.9 26 A ASN C 130 184.2 134.3 20.5 21 A ASN O 130 184.6 134.8 19.5 21 A TYR N 131 183.9 133.0 20.6 22 A TYR CA 131 184.0 132.0 19.5 21 A TYR CB 131 183.8 130.6 19.9 20 A TYR CG 131 182.5 130.3 20.6 20 A TYR CD1 131 181.4 130.0 19.8 19 A TYR CE1 131 180.1 129.9 20.4 19 A TYR CD2 131 182.3 130.5 22.0 19 A TYR CE2 131 181.1 130.4 22.6 19 A TYR CZ 131 179.9 130.1 21.8 20 A TYR OH 131 178.7 130.0 22.4 20 A TYR C 131 183.1 132.3 18.3 23 A TYR O 131 183.3 131.8 17.2 26 A THR N 132 182.0 133.1 18.5 23 A THR CA 132 181.1 133.5 17.5 22 A THR CB 132 179.8 134.1 18.1 23 A THR OG1 132 179.1 133.1 18.8 24 A THR CG2 132 178.9 134.6 17.0 24 A THR C 132 181.7 134.5 16.6 22 A THR O 132 181.6 134.5 15.4 23 A VAL N 133 182.4 135.4 17.2 22 A VAL CA 133 183.1 136.5 16.4 22 A VAL CB 133 183.7 137.6 17.3 22 A VAL CG1 133 184.4 138.6 16.4 22 A VAL CG2 133 182.5 138.4 18.0 21 A VAL C 133 184.2 135.8 15.6 23 A VAL O 133 184.4 136.1 14.5 25 A TRP N 134 185.0 134.9 16.3 23 A TRP CA 134 186.1 134.2 15.7 24 A TRP CB 134 186.8 133.3 16.6 21 A TRP CG 134 187.8 133.9 17.5 19 A TRP CD2 134 189.1 134.5 17.0 19 A TRP CE2 134 189.8 135.0 18.1 18 A TRP CE3 134 189.7 134.6 15.7 19 A TRP CD1 134 187.8 134.2 18.8 19 A TRP NE1 134 189.0 134.8 19.2 18 A TRP CZ2 134 191.0 135.6 18.0 19 A TRP CZ3 134 190.9 135.2 15.6 19 A TRP CH2 134 191.6 135.7 16.7 20 A TRP C 134 185.6 133.5 14.4 26 A TRP O 134 186.2 133.5 13.4 27 A HIS N 135 184.4 132.9 14.5 28 A HIS CA 135 183.8 132.1 13.4 31 A HIS CB 135 182.6 131.4 13.9 33 A HIS CG 135 181.8 130.7 12.8 35 A HIS CD2 135 181.0 131.2 11.9 36 A HIS ND1 135 181.8 129.4 12.6 36 A HIS CE1 135 181.1 129.1 11.5 37 A HIS NE2 135 180.6 130.2 11.1 36 A HIS C 135 183.4 133.0 12.3 32 A HIS O 135 183.7 132.7 11.1 32 A PHE N 136 182.7 134.1 12.6 31 A PHE CA 136 182.4 135.1 11.6 30 A PHE CB 136 181.5 136.2 12.2 32 A PHE CG 136 181.0 137.2 11.2 34 A PHE CD1 136 180.0 136.8 10.2 35 A PHE CD2 136 181.4 138.5 11.1 35 A PHE CE1 136 179.5 137.6 9.2 35 A PHE CE2 136 180.9 139.4 10.2 35 A PHE CZ 136 180.0 139.0 9.2 35 A PHE C 136 183.6 135.7 10.9 29 A PHE O 136 183.6 135.9 9.7 30 A ARG N 137 184.7 135.9 11.6 27 A ARG CA 137 185.9 136.4 11.0 26 A ARG CB 137 187.0 136.7 12.1 25 A ARG CG 137 188.2 137.3 11.5 23 A ARG CD 137 189.3 137.5 12.6 22 A ARG NE 137 190.5 138.2 12.1 22 A ARG CZ 137 190.6 139.5 11.9 21 A ARG NH1 137 189.6 140.3 12.2 21 A ARG NH2 137 191.8 139.9 11.5 21 A ARG C 137 186.4 135.4 10.0 26 A ARG O 137 186.9 135.8 9.0 27 A ARG N 138 186.3 134.1 10.3 26 A ARG CA 138 186.8 133.1 9.3 25 A ARG CB 138 186.8 131.7 10.0 25 A ARG CG 138 188.2 131.0 10.0 23 A ARG CD 138 188.6 130.8 11.4 22 A ARG NE 138 187.7 129.9 12.1 21 A ARG CZ 138 187.6 129.9 13.5 21 A ARG NH1 138 188.4 130.6 14.2 20 A ARG NH2 138 186.7 129.2 14.1 20 A ARG C 138 185.9 133.2 8.1 26 A ARG O 138 186.4 133.1 7.0 25 A VAL N 139 184.6 133.4 8.3 26 A VAL CA 139 183.7 133.5 7.2 27 A VAL CB 139 182.2 133.8 7.7 27 A VAL CG1 139 181.3 134.2 6.6 26 A VAL CG2 139 181.7 132.6 8.5 26 A VAL C 139 184.1 134.7 6.2 28 A VAL O 139 184.3 134.5 5.0 28 A LEU N 140 184.4 135.8 6.8 28 A LEU CA 140 184.8 137.0 6.1 27 A LEU CB 140 184.9 138.2 7.0 27 A LEU CG 140 183.5 138.6 7.5 28 A LEU CD1 140 183.6 139.7 8.5 28 A LEU CD2 140 182.7 139.0 6.3 27 A LEU C 140 186.2 136.7 5.4 29 A LEU O 140 186.4 137.2 4.3 29 A LEU N 141 187.0 136.0 6.1 30 A LEU CA 141 188.4 135.7 5.6 31 A LEU CB 141 189.1 134.8 6.5 29 A LEU CG 141 189.9 135.4 7.7 27 A LEU CD1 141 190.7 134.3 8.4 25 A LEU CD2 141 190.9 136.4 7.2 26 A LEU C 141 188.2 134.9 4.3 34 A LEU O 141 189.0 135.1 3.4 34 A ARG N 142 187.1 134.1 4.2 38 A ARG CA 142 186.8 133.4 3.0 42 A ARG CB 142 185.8 132.2 3.3 46 A ARG CG 142 186.3 131.3 4.4 50 A ARG CD 142 185.2 130.4 5.0 53 A ARG NE 142 185.2 130.3 6.5 57 A ARG CZ 142 184.6 129.4 7.2 57 A ARG NH1 142 183.9 128.4 6.7 59 A ARG NH2 142 184.7 129.4 8.6 57 A ARG C 142 186.1 134.3 1.9 42 A ARG O 142 186.6 134.4 0.8 41 A SER N 143 185.1 135.0 2.3 41 A SER CA 143 184.4 135.8 1.4 42 A SER CB 143 183.2 136.5 2.0 41 A SER OG 143 182.4 135.4 2.7 44 A SER C 143 185.2 136.9 0.7 42 A SER O 143 185.2 137.1 −0.5 44 A LEU N 144 185.9 137.7 1.6 41 A LEU CA 144 186.7 138.8 1.0 41 A LEU CB 144 186.9 139.9 2.1 39 A LEU CG 144 185.9 140.1 3.2 38 A LEU CD1 144 186.3 141.2 4.1 38 A LEU CD2 144 184.5 140.5 2.6 37 A LEU C 144 188.1 138.4 0.5 41 A LEU O 144 188.9 139.2 0.0 43 A GLN N 145 188.3 137.0 0.5 42 A GLN CA 145 189.6 136.5 0.0 41 A GLN CB 145 189.7 136.4 −1.5 45 A GLN CG 145 188.7 135.4 −2.0 49 A GLN CD 145 188.8 135.3 −3.5 52 A GLN OE1 145 188.6 136.3 −4.2 54 A GLN NE2 145 189.0 134.1 −4.0 54 A GLN C 145 190.8 137.3 0.6 39 A GLN O 145 191.5 137.9 −0.2 39 A LYS N 146 190.9 137.3 1.9 37 A LYS CA 146 191.9 138.1 2.6 35 A LYS CB 146 191.5 138.2 4.0 35 A LYS CG 146 190.2 139.0 4.3 35 A LYS CD 146 190.3 140.4 3.7 35 A LYS CE 146 191.4 141.2 4.3 36 A LYS NZ 146 191.3 142.6 3.7 36 A LYS C 146 193.2 137.3 2.5 34 A LYS O 146 193.2 136.1 2.4 33 A ASP N 147 194.3 138.0 2.5 35 A ASP CA 147 195.6 137.5 2.5 34 A ASP CB 147 196.7 138.6 2.3 34 A ASP CG 147 198.1 138.0 2.2 34 A ASP OD1 147 198.5 137.2 3.1 35 A ASP OD2 147 198.8 138.4 1.3 36 A ASP C 147 195.8 136.8 3.8 35 A ASP O 147 195.8 137.4 4.9 35 A LEU N 148 195.8 135.4 3.8 34 A LEU CA 148 196.0 134.6 5.0 31 A LEU CB 148 195.6 133.1 4.7 30 A LEU CG 148 194.2 132.9 4.2 29 A LEU CD1 148 193.9 131.5 4.0 30 A LEU CD2 148 193.2 133.4 5.2 29 A LEU C 148 197.4 134.7 5.6 31 A LEU O 148 197.5 134.3 6.8 31 A GLN N 149 198.4 135.1 4.9 31 A GLN CA 149 199.7 135.2 5.5 32 A GLN CB 149 200.8 135.3 4.5 34 A GLN CG 149 202.1 134.7 5.0 36 A GLN CD 149 202.0 133.4 5.7 38 A GLN OE1 149 201.7 132.4 5.1 38 A GLN NE2 149 202.2 133.4 7.0 38 A GLN C 149 199.7 136.4 6.4 33 A GLN O 149 200.5 136.5 7.3 34 A GLU N 150 198.9 137.4 6.1 34 A GLU CA 150 198.8 138.6 6.8 35 A GLU CB 150 198.0 139.7 6.0 38 A GLU CG 150 199.0 140.8 5.5 44 A GLU CD 150 200.2 140.3 4.7 47 A GLU OE1 150 201.3 140.6 5.2 49 A GLU OE2 150 200.0 139.7 3.7 48 A GLU C 150 198.0 138.2 8.1 33 A GLU O 150 198.3 138.7 9.2 33 A GLU N 151 197.0 137.4 7.9 31 A GLU CA 151 196.2 136.9 9.0 30 A GLU CB 151 195.0 136.1 8.5 29 A GLU CG 151 194.0 135.6 9.6 28 A GLU CD 151 193.2 136.7 10.4 28 A GLU OE1 151 193.4 137.9 10.1 28 A GLU OE2 151 192.4 136.3 11.2 27 A GLU C 151 197.1 136.0 10.0 29 A GLU O 151 196.9 136.1 11.2 30 A MET N 152 198.0 135.3 9.4 28 A MET CA 152 198.9 134.5 10.3 27 A MET CB 152 199.9 133.8 9.4 27 A MET CG 152 199.4 132.5. 8.9 28 A MET SD 152 199.4 131.2 10.2 28 A MET CE 152 201.0 130.6 10.1 29 A MET C 152 199.6 135.5 11.2 27 A MET O 152 199.8 135.3 12.4 27 A ASN N 153 200.0 136.7 10.6 26 A ASN CA 153 200.7 137.7 11.3 27 A ASN CB 153 201.1 138.8 10.4 28 A ASN CG 153 202.1 138.4 9.3 29 A ASN OD1 153 202.6 137.3 9.3 28 A ASN ND2 153 202.4 139.4 8.4 30 A ASN C 153 199.9 138.2 12.5 26 A ASN O 153 200.4 138.3 13.6 24 A TYR N 154 198.6 138.4 12.2 25 A TYR CA 154 197.6 138.8 13.2 25 A TYR CB 154 196.3 139.1 12.5 24 A TYR CG 154 195.2 139.4 13.4 26 A TYR CD1 154 195.1 140.6 14.1 26 A TYR CE1 154 194.1 140.8 15.1 25 A TYR CD2 154 194.2 138.4 13.6 27 A TYR CE2 154 193.2 138.6 14.5 27 A TYR CZ 154 193.2 139.8 15.3 26 A TYR OH 154 192.2 140.0 16.2 28 A TYR C 154 197.5 137.8 14.3 25 A TYR O 154 197.7 138.2 15.5 26 A ILE N 155 197.2 136.6 14.0 24 A ILE CA 155 197.0 135.5 15.0 22 A ILE CB 155 196.4 134.2 14.4 21 A ILE CG2 155 197.5 133.4 13.8 21 A ILE CG1 155 195.7 133.4 15.5 20 A ILE CD1 155 194.5 134.2 16.0 19 A ILE C 155 198.3 135.3 15.8 20 A ILE O 155 198.2 135.0 17.0 20 A THR N 156 199.4 135.6 15.2 20 A THR CA 156 200.7 135.4 15.9 20 A THR CB 156 201.8 135.7 14.9 21 A THR OG1 156 201.8 134.6 13.9 21 A THR CG2 156 203.2 135.7 15.6 20 A THR C 156 200.7 136.4 17.1 22 A THR O 156 201.1 136.1 18.2 22 A ALA N 157 200.3 137.7 16.8 23 A ALA CA 157 200.4 138.8 17.7 23 A ALA CB 157 200.0 140.1 17.1 21 A ALA C 157 199.4 138.5 18.9 23 A ALA O 157 199.8 138.6 20.1 24 A ILE N 158 198.2 138.2 18.5 23 A ILE CA 158 197.1 137.9 19.5 23 A ILE CB 158 195.8 137.6 18.8 23 A ILE CG2 158 194.7 137.2 19.8 24 A ILE CG1 158 195.4 138.7 18.0 24 A ILE CD1 158 195.0 140.0 18.8 25 A ILE C 158 197.5 136.7 20.4 23 A ILE O 158 197.2 136.8 21.6 24 A ILE N 159 198.0 135.6 19.9 21 A ILE CA 159 198.4 134.5 20.7 21 A ILE CB 159 198.9 133.3 19.9 20 A ILE CG2 159 199.4 132.2 20.8 18 A ILE CG1 159 197.7 132.7 19.1 19 A ILE CD1 159 198.2 131.6 18.1 17 A ILE C 159 199.5 135.0 21.7 22 A ILE O 159 199.5 134.7 22.9 21 A GLU N 160 200.5 135.7 21.2 23 A GLU CA 160 201.6 136.1 22.0 24 A GLU CB 160 202.6 137.0 21.3 24 A GLU CG 160 203.4 136.3 20.2 23 A GLU CD 160 204.6 135.6 20.6 24 A GLU OE1 160 205.0 135.8 21.8 23 A GLU OE2 160 205.3 135.0 19.8 23 A GLU C 160 201.0 136.9 23.2 26 A GLU O 160 201.5 136.8 24.3 27 A GLU N 161 200.0 137.8 23.0 26 A GLU CA 161 199.4 138.5 24.1 29 A GLU CB 161 198.8 139.8 23.6 30 A GLU CG 161 197.8 139.8 22.6 34 A GLU CD 161 197.6 141.1 21.8 36 A GLU OE1 161 198.7 141.7 21.4 37 A GLU OE2 161 196.5 141.5 21.6 38 A GLU C 161 198.5 137.7 25.0 28 A GLU O 161 198.5 137.9 26.2 29 A GLN N 162 197.8 136.7 24.5 27 A GLN CA 162 197.0 135.8 25.3 26 A GLN CB 162 195.5 136.4 25.4 29 A GLN CG 162 194.8 136.9 24.2 33 A GLN CD 162 193.6 137.7 24.6 35 A GLN OE1 162 192.8 137.4 25.6 34 A GLN NE2 162 193.4 138.9 23.9 36 A GLN C 162 197.0 134.4 24.8 23 A GLN O 162 196.1 133.9 24.1 23 A PRO N 163 198.1 133.6 25.2 20 A PRO CD 163 199.1 134.1 26.1 17 A PRO CA 163 198.3 132.3 24.8 18 A PRO CB 163 199.8 132.1 25.0 17 A PRO CG 163 200.0 132.9 26.3 17 A PRO C 163 197.5 131.2 25.5 19 A PRO O 163 197.7 130.0 25.2 19 A LYS N 164 196.7 131.6 26.4 20 A LYS CA 164 195.9 130.6 27.1 20 A LYS CB 164 196.1 130.7 28.7 20 A LYS CG 164 197.4 130.2 29.1 22 A LYS CD 164 197.5 130.0 30.6 22 A LYS CE 164 198.9 129.6 31.0 23 A LYS NZ 164 198.9 129.4 32.5 24 A LYS C 164 194.4 131.0 26.8 20 A LYS O 164 193.8 131.7 27.5 21 A ASN N 165 194.1 130.6 25.6 20 A ASN CA 165 192.8 130.9 25.0 19 A ASN CB 165 192.8 132.2 24.3 20 A ASN CG 165 191.5 132.5 23.5 21 A ASN OD1 165 191.2 131.9 22.6 22 A ASN ND2 165 190.8 133.6 24.0 22 A ASN C 165 192.6 129.8 24.0 18 A ASN O 165 193.6 129.4 23.3 19 A TYR N 166 191.4 129.2 23.9 18 A TYR CA 166 191.1 128.1 23.0 17 A TYR CB 166 189.9 127.3 23.5 17 A TYR CG 166 190.2 126.3 24.6 18 A TYR CD1 166 189.8 126.6 25.9 18 A TYR CE1 166 190.0 125.7 27.0 18 A TYR CD2 166 190.8 125.1 24.4 18 A TYR CE2 166 191.0 124.1 25.4 19 A TYR CZ 166 190.6 124.5 26.7 18 A TYR OH 166 190.7 123.6 27.8 18 A TYR C 166 190.9 128.5 21.6 18 A TYR O 166 191.3 127.8 20.6 18 A GLN N 167 190.3 129.7 21.4 17 A GLN CA 167 189.9 130.2 20.1 17 A GLN CB 167 188.9 131.3 20.2 16 A GLN CG 167 187.5 130.9 20.6 16 A GLN CD 167 187.4 130.5 22.1 19 A GLN OE1 167 188.1 131.0 22.9 20 A GLN NE2 167 186.6 129.5 22.4 19 A GLN C 167 191.1 130.6 19.2 16 A GLN O 167 191.1 130.4 18.0 17 A VAL N 168 192.1 131.3 19.9 16 A VAL CA 168 193.2 131.8 19.2 15 A VAL CB 168 194.1 132.7 20.0 14 A VAL CG1 168 193.4 134.0 20.5 12 A VAL CG2 168 194.7 132.0 21.2 13 A VAL C 168 194.0 130.6 18.6 17 A VAL O 168 194.3 130.6 17.4 20 A TRP N 169 194.3 129.6 19.4 17 A TRP CA 169 195.0 128.5 18.8 16 A TRP CB 169 195.5 127.5 19.9 15 A TRP CG 169 196.5 128.1 20.8 15 A TRP CD2 169 197.9 128.1 20.5 14 A TRP CE2 169 198.6 128.8 21.6 14 A TRP CE3 169 198.7 127.6 19.4 14 A TRP CD1 169 196.4 128.8 22.0 15 A TRP NE1 169 197.6 129.1 22.5 15 A TRP CZ2 169 200.0 128.9 21.6 14 A TRP CZ3 169 200.1 127.8 19.5 14 A TRP CH2 169 200.7 128.4 20.6 14 A TRP C 169 194.3 127.7 17.8 16 A TRP O 169 194.9 127.3 16.8 15 A HIS N 170 193.0 127.6 17.9 17 A HIS CA 170 192.2 126.9 16.9 19 A HIS CB 170 190.8 126.6 17.3 19 A HIS CG 170 190.0 125.8 16.3 20 A HIS CD2 170 189.0 126.2 15.4 21 A HIS ND1 170 190.3 124.5 15.9 20 A HIS CE1 170 189.5 124.1 14.9 21 A HIS NE2 170 188.7 125.2 14.6 21 A HIS C 170 192.2 127.7 15.6 20 A HIS O 170 192.1 127.1 14.5 20 A HIS N 171 192.1 129.0 15.7 20 A HIS CA 171 192.1 129.9 14.6 20 A HIS CB 171 191.9 131.3 15.0 19 A HIS CG 171 191.8 132.3 13.8 20 A HIS CD2 171 192.7 133.1 13.2 19 A HIS ND1 171 190.6 132.5 13.2 19 A HIS CE1 171 190.8 133.4 12.2 18 A HIS NE2 171 192.0 133.8 12.3 18 A HIS C 171 193.4 129.7 13.8 20 A HIS O 171 193.4 129.6 12.6 22 A ARG N 172 194.5 129.6 14.6 20 A ARG CA 172 195.8 129.4 14.0 19 A ARG CB 172 196.9 129.5 15.0 16 A ARG CG 172 198.3 129.3 14.4 14 A ARG CD 172 199.4 129.8 15.2 14 A ARG NE 172 200.6 129.7 14.5 14 A ARG CZ 172 201.4 130.8 14.3 15 A ARG NH1 172 201.0 132.0 14.7 15 A ARG NH2 172 202.6 130.6 13.6 16 A ARG C 172 195.9 128.1 13.2 20 A ARG O 172 196.6 128.1 12.2 23 A ARG N 173 195.3 127.1 13.7 21 A ARG CA 173 195.3 125.8 13.1 21 A ARG CB 173 194.8 124.7 14.0 23 A ARG CG 173 194.4 123.4 13.3 26 A ARG CD 173 193.9 122.4 14.3 31 A ARG NE 173 193.3 121.3 13.6 34 A ARG CZ 173 193.3 120.0 14.1 36 A ARG NH1 173 193.9 119.7 15.2 37 A ARG NH2 173 192.7 119.1 13.4 38 A ARG C 173 194.5 125.8 11.8 22 A ARG O 173 194.9 125.2 10.9 23 A VAL N 174 193.4 126.5 11.8 23 A VAL CA 174 192.6 126.6 10.6 24 A VAL CB 174 191.3 127.3 10.9 23 A VAL CG1 174 190.5 127.5 9.6 23 A VAL CG2 174 190.4 126.5 11.8 21 A VAL C 174 193.4 127.2 9.5 25 A VAL O 174 193.3 126.7 8.3 27 A LEU N 175 194.2 128.3 9.8 25 A LEU CA 175 194.9 129.0 8.8 24 A LEU CB 175 195.6 130.2 9.3 22 A LEU CG 175 194.7 131.3 9.9 22 A LEU CD1 175 195.6 132.5 10.5 20 A LEU CD2 175 193.7 131.9 8.9 20 A LEU C 175 196.0 128.1 8.2 25 A LEU O 175 196.2 128.1 7.0 26 A VAL N 176 196.7 127.4 9.1 26 A VAL CA 176 197.8 126.4 8.6 25 A VAL CB 176 198.5 125.8 9.9 25 A VAL CG1 176 199.4 124.7 9.4 25 A VAL CG2 176 199.3 126.9 10.6 24 A VAL C 176 197.2 125.3 7.8 25 A VAL O 176 197.9 124.8 6.9 25 A GLU N 177 196.0 124.9 8.0 26 A GLU CA 177 195.3 123.9 7.2 27 A GLU CB 177 194.1 123.5 7.9 27 A GLU CG 177 194.3 122.6 9.1 28 A GLU CD 177 193.0 122.2 9.8 30 A GLU OE1 177 193.1 121.2 10.6 30 A GLU OE2 177 192.0 122.9 9.7 31 A GLU C 177 195.0 124.5 5.9 27 A GLU O 177 195.5 124.0 4.8 29 A TRP N 178 194.4 125.6 5.8 27 A TRP CA 178 194.0 126.3 4.6 26 A TRP CB 178 193.4 127.7 5.0 25 A TRP CG 178 192.0 127.7 5.3 22 A TRP CD2 178 191.2 128.7 5.9 21 A TRP CE2 178 189.9 128.3 6.0 20 A TRP CE3 178 191.5 130.1 6.2 20 A TRP CD1 178 191.1 126.6 5.2 21 A TRP NE1 178 189.9 127.0 5.6 21 A TRP CZ2 178 188.9 129.1 6.5 20 A TRP CZ3 178 190.5 130.9 6.7 20 A TRP CH2 178 189.2 130.4 6.9 20 A TRP C 178 195.2 126.5 3.7 28 A TRP O 178 195.3 126.0 2.6 30 A LEU N 179 196.3 127.1 4.3 29 A LEU CA 179 197.5 127.3 3.6 30 A LEU CB 179 198.4 128.3 4.3 31 A LEU CG 179 197.8 129.7 4.7 32 A LEU CD1 179 198.8 130.4 5.6 31 A LEU CD2 179 197.6 130.5 3.4 32 A LEU C 179 198.4 126.0 3.4 32 A LEU O 179 199.3 126.1 2.6 33 A LYS N 180 198.1 125.0 4.1 34 A LYS CA 180 198.9 123.8 4.0 34 A LYS CB 180 198.8 123.2 2.7 35 A LYS CG 180 197.4 122.6 2.5 38 A LYS CD 180 196.9 122.9 1.1 40 A LYS CE 180 195.5 122.3 1.0 42 A LYS NZ 180 195.4 120.9 1.4 42 A LYS C 180 200.4 124.2 4.3 34 A LYS O 180 201.3 123.8 3.6 35 A ASP N 181 200.6 125.1 5.2 34 A ASP CA 181 201.9 125.7 5.5 34 A ASP CB 181 202.0 127.1 5.0 33 A ASP CG 181 203.4 127.7 4.9 33 A ASP OD1 181 204.3 126.9 5.2 33 A ASP OD2 181 203.5 128.8 4.5 34 A ASP C 181 202.3 125.6 6.9 35 A ASP O 181 201.9 126.4 7.8 35 A PRO N 182 203.2 124.6 7.3 34 A PRO CD 182 203.5 123.4 6.5 34 A PRO CA 182 203.7 124.5 8.7 34 A PRO CB 182 203.8 123.0 8.8 35 A PRO CG 182 204.4 122.6 7.4 33 A PRO C 182 205.0 125.1 8.9 34 A PRO O 182 205.6 124.9 9.9 36 A SER N 183 205.5 125.8 7.9 34 A SER CA 183 206.9 126.4 8.0 34 A SER CB 183 207.3 127.0 6.7 35 A SER OG 183 206.5 128.1 6.4 38 A SER C 183 207.2 127.3 9.2 34 A SER O 183 208.3 127.3 9.6 35 A GLN N 184 206.3 128.1 9.7 33 A GLN CA 184 206.6 128.9 10.8 32 A GLN CB 184 206.2 130.4 10.5 34 A GLN CG 184 204.8 130.6 10.1 37 A GLN CD 184 204.5 132.0 9.5 38 A GLN OE1 184 204.5 133.0 10.2 38 A GLN NE2 184 204.3 132.0 8.2 37 A GLN C 184 206.1 128.5 12.2 30 A GLN O 184 206.4 129.1 13.2 30 A GLU N 185 205.6 127.3 12.2 26 A GLU CA 185 205.0 126.7 13.4 24 A GLU CB 185 204.1 125.5 13.1 22 A GLU CG 185 202.9 125.8 12.2 21 A GLU CD 185 202.2 127.1 12.6 22 A GLU OE1 185 201.3 127.0 13.4 22 A GLU OE2 185 202.5 128.2 12.0 23 A GLU C 185 206.0 126.3 14.6 23 A GLU O 185 205.8 126.8 15.7 23 A LEU N 186 206.9 125.5 14.3 22 A LEU CA 186 207.8 125.1 15.4 23 A LEU CB 186 208.8 124.0 14.9 21 A LEU CG 186 208.2 122.7 14.4 21 A LEU CD1 186 209.3 121.7 14.0 21 A LEU CD2 186 207.3 122.1 15.4 19 A LEU C 186 208.6 126.2 16.0 25 A LEU O 186 208.8 126.3 17.2 27 A GLU N 187 208.9 127.2 15.2 26 A GLU CA 187 209.6 128.4 15.6 27 A GLU CB 187 210.1 129.2 14.5 31 A GLU CG 187 210.7 130.5 14.8 35 A GLU CD 187 211.4 131.2 13.6 38 A GLU OE1 187 211.4 130.7 12.5 40 A GLU OE2 187 212.1 132.2 13.9 40 A GLU C 187 208.6 129.3 16.5 26 A GLU O 187 209.0 129.8 17.5 26 A PHE N 188 207.4 129.6 16.0 23 A PHE CA 188 206.4 130.4 16.7 22 A PHE CB 188 205.2 130.5 15.9 21 A PHE CG 188 204.0 131.0 16.7 21 A PHE CD1 188 204.1 132.3 17.3 21 A PHE CD2 188 203.0 130.2 17.0 21 A PHE CE1 188 203.0 132.8 18.1 20 A PHE CE2 188 201.9 130.7 17.8 21 A PHE CZ 188 202.0 132.0 18.3 20 A PHE C 188 206.1 129.7 18.0 21 A PHE O 188 206.1 130.4 19.1 22 A ILE N 189 205.8 128.4 18.0 22 A ILE CA 189 205.5 127.6 19.2 23 A ILE CB 189 205.2 126.2 18.9 21 A ILE CG2 189 204.8 125.4 20.1 21 A ILE CG1 189 203.9 126.2 18.0 20 A ILE CD1 189 203.6 124.8 17.4 19 A ILE C 189 206.7 127.7 20.2 23 A ILE O 189 206.5 127.8 21.5 24 A ALA N 190 207.9 127.6 19.7 23 A ALA CA 190 209.1 127.7 20.6 23 A ALA CB 190 210.4 127.4 19.8 22 A ALA C 190 209.2 129.0 21.2 23 A ALA O 190 209.8 129.2 22.3 24 A ASP N 191 208.7 130.1 20.6 25 A ASP CA 191 208.7 131.4 21.2 26 A ASP CB 191 208.5 132.5 20.2 28 A ASP CG 191 208.6 133.9 20.9 32 A ASP OD1 191 209.7 134.2 21.4 33 A ASP OD2 191 207.5 134.6 20.9 33 A ASP C 191 207.7 131.5 22.3 25 A ASP O 191 208.0 132.2 23.3 27 A ILE N 192 206.5 130.9 22.2 23 A ILE CA 192 205.5 130.9 23.2 22 A ILE CB 192 204.2 130.3 22.7 20 A ILE CG2 192 203.2 130.2 23.8 20 A ILE CG1 192 203.7 131.2 21.5 19 A ILE CD1 192 203.2 132.5 22.0 19 A ILE C 192 206.0 130.1 24.4 22 A ILE O 192 205.9 130.5 25.6 22 A LEU N 193 206.5 128.9 24.1 23 A LEU CA 193 207.1 128.0 25.1 24 A LEU CB 193 207.5 126.6 24.6 21 A LEU CG 193 206.3 125.8 24.0 21 A LEU CD1 193 206.9 124.5 23.4 21 A LEU CD2 193 205.3 125.5 25.1 20 A LEU C 193 208.3 128.6 25.8 25 A LEU O 193 208.8 128.1 26.8 27 A ASN N 194 208.8 129.6 25.2 25 A ASN CA 194 210.0 130.3 25.8 26 A ASN CB 194 210.8 131.0 24.7 28 A ASN CG 194 212.0 131.7 25.3 30 A ASN OD1 194 212.1 132.9 25.4 33 A ASN ND2 194 213.0 130.9 25.8 30 A ASN C 194 209.5 131.2 26.9 27 A ASN O 194 210.3 131.6 27.8 28 A GLN N 195 208.2 131.6 26.8 26 A GLN CA 195 207.6 132.5 27.8 25 A GLN CB 195 206.6 133.4 27.0 26 A GLN CG 195 207.4 134.2 26.0 27 A GLN CD 195 206.5 134.9 25.0 27 A GLN OE1 195 205.7 135.7 25.3 29 A GLN NE2 195 206.7 134.6 23.7 27 A GLN C 195 206.9 131.7 28.9 25 A GLN O 195 206.9 132.1 30.0 27 A ASP N 196 206.3 130.6 28.5 23 A ASP CA 196 205.6 129.6 29.4 19 A ASP CB 196 204.1 129.9 29.5 18 A ASP CG 196 203.4 128.9 30.4 17 A ASP OD1 196 204.0 128.0 30.9 17 A ASP OD2 196 202.2 129.0 30.5 17 A ASP C 196 205.9 128.3 28.8 19 A ASP O 196 205.2 127.8 27.9 20 A ALA N 197 206.9 127.6 29.3 18 A ALA CA 197 207.3 126.3 28.9 18 A ALA CB 197 208.7 125.9 29.5 18 A ALA C 197 206.3 125.2 29.1 18 A ALA O 197 206.6 124.0 28.7 18 A LYS N 198 205.2 125.4 29.7 18 A LYS CA 198 204.2 124.4 29.9 18 A LYS CB 198 204.1 124.1 31.4 19 A LYS CG 198 205.5 123.7 32.0 22 A LYS CD 198 205.4 123.6 33.5 21 A LYS CE 198 206.7 123.1 34.1 22 A LYS NZ 198 206.5 122.6 35.5 22 A LYS C 198 202.9 124.7 29.4 18 A LYS O 198 201.9 124.1 29.8 20 A ASN N 199 202.8 125.7 28.5 18 A ASN CA 199 201.5 126.1 27.9 18 A ASN CB 199 201.7 127.3 27.0 18 A ASN CG 199 200.3 127.8 26.4 19 A ASN OD1 199 199.7 127.1 25.6 20 A ASN ND2 199 199.9 129.0 26.8 18 A ASN C 199 200.9 124.9 27.2 20 A ASN O 199 201.5 124.3 26.3 23 A TYR N 200 199.8 124.5 27.7 19 A TYR CA 200 199.1 123.3 27.2 19 A TYR CB 200 197.9 123.0 28.0 18 A TYR CG 200 197.5 121.6 28.0 19 A TYR CD1 200 197.9 120.7 29.0 19 A TYR CE1 200 197.6 119.3 29.0 18 A TYR CD2 200 196.6 121.1 27.0 18 A TYR CE2 200 196.3 119.8 27.0 17 A TYR CZ 200 196.8 118.9 27.9 17 A TYR OH 200 196.4 117.6 27.8 15 A TYR C 200 198.7 123.4 25.7 18 A TYR O 200 199.0 122.4 25.0 18 A HIS N 201 198.1 124.5 25.3 17 A HIS CA 201 197.7 124.7 24.0 17 A HIS CB 201 197.0 126.0 23.9 16 A HIS CG 201 195.9 126.2 24.9 16 A HIS CD2 201 196.0 126.9 26.1 14 A HIS ND1 201 194.6 125.7 24.8 14 A HIS CE1 201 193.9 126.1 25.9 14 A HIS NE2 201 194.7 126.7 26.7 13 A HIS C 201 198.9 124.7 23.0 16 A HIS O 201 198.8 124.1 21.9 16 A ALA N 202 200.0 125.3 23.4 17 A ALA CA 202 201.2 125.4 22.6 17 A ALA CB 202 202.2 126.2 23.3 17 A ALA C 202 201.8 124.0 22.3 19 A ALA O 202 202.1 123.7 21.2 22 A TRP N 203 201.9 123.2 23.4 19 A TRP CA 203 202.4 121.8 23.3 17 A TRP CB 203 202.5 121.2 24.7 16 A TRP CG 203 203.7 121.6 25.4 15 A TRP CD2 203 205.0 121.3 24.9 15 A TRP CE2 203 205.9 121.9 25.9 15 A TRP CE3 203 205.6 120.6 23.9 15 A TRP CD1 203 203.8 122.3 26.5 14 A TRP NE1 203 205.1 122.5 26.8 15 A TRP CZ2 203 207.3 121.8 25.8 15 A TRP CZ3 203 207.0 120.5 23.8 15 A TRP CH2 203 207.8 121.1 24.7 15 A TRP C 203 201.5 121.0 22.4 19 A TRP O 203 201.9 120.2 21.5 20 A GLN N 204 200.1 121.1 22.6 20 A GLN CA 204 199.1 120.4 21.8 20 A GLN CB 204 197.8 120.6 22.4 20 A GLN CG 204 196.7 119.8 21.8 20 A GLN CD 204 195.3 120.0 22.5 21 A GLN OE1 204 194.3 120.1 21.8 22 A GLN NE2 204 195.4 120.0 23.8 21 A GLN C 204 199.2 120.8 20.3 21 A GLN O 204 199.0 120.0 19.4 20 A HIS N 205 199.4 122.1 20.1 20 A HIS CA 205 199.4 122.6 18.7 20 A HIS CB 205 199.5 124.1 18.7 19 A HIS CG 205 199.4 124.7 17.3 19 A HIS CD2 205 200.3 125.4 16.6 18 A HIS ND1 205 198.3 124.6 16.6 19 A HIS CE1 205 198.4 125.2 15.4 17 A HIS NE2 205 199.7 125.7 15.4 17 A HIS C 205 200.7 122.0 18.1 21 A HIS O 205 200.7 121.5 17.0 24 A ARG N 206 201.8 122.0 18.9 21 A ARG CA 206 203.1 121.5 18.4 20 A ARG CB 206 204.1 121.6 19.5 19 A ARG CG 206 205.6 121.5 19.1 18 A ARG CD 206 206.6 121.9 20.1 18 A ARG NE 206 207.9 121.9 19.5 20 A ARG CZ 206 208.6 122.9 19.0 21 A ARG NH1 206 208.0 124.1 19.0 21 A ARG NH2 206 209.8 122.7 18.5 21 A ARG C 206 202.9 120.0 18.0 21 A ARG O 206 203.4 119.6 17.0 22 A GLN N 207 202.2 119.2 18.8 20 A GLN CA 207 202.0 117.8 18.5 20 A GLN CB 207 201.4 117.0 19.6 19 A GLN CG 207 202.2 116.9 20.9 20 A GLN CD 207 201.6 115.9 21.8 20 A GLN OE1 207 200.5 115.4 21.7 20 A GLN NE2 207 202.5 115.5 22.8 19 A GLN C 207 201.2 117.6 17.2 21 A GLN O 207 201.5 116.7 16.4 22 A TRP N 208 200.2 118.4 17.0 21 A TRP CA 208 199.4 118.3 15.8 22 A TRP CB 208 198.2 119.3 15.9 20 A TRP CG 208 197.4 119.4 14.6 20 A TRP CD2 208 197.5 120.5 13.7 20 A TRP CE2 208 196.7 120.2 12.6 19 A TRP CE3 208 198.2 121.7 13.6 21 A TRP CD1 208 196.6 118.5 14.1 20 A TRP NE1 208 196.1 119.0 12.9 20 A TRP CZ2 208 196.6 121.0 11.5 19 A TRP CZ3 208 198.1 122.5 12.5 20 A TRP CH2 208 197.3 122.2 11.5 19 A TRP C 208 200.2 118.7 14.5 23 A TRP O 208 200.1 118.0 13.5 24 A VAL N 209 201.0 119.8 14.6 24 A VAL CA 209 201.8 120.2 13.4 24 A VAL CB 209 202.5 121.5 13.7 24 A VAL CG1 209 203.3 121.9 12.5 25 A VAL CG2 209 201.5 122.6 14.0 25 A VAL C 209 202.8 119.1 13.1 25 A VAL O 209 203.0 118.7 11.9 26 A ILE N 210 203.5 118.6 14.1 26 A ILE CA 210 204.5 117.5 13.9 25 A ILE CB 210 205.2 117.2 15.2 24 A ILE CG2 210 206.2 116.0 15.0 24 A ILE CG1 210 206.1 118.3 15.7 23 A ILE CD1 210 206.8 118.0 16.9 22 A ILE C 210 203.9 116.3 13.4 27 A ILE O 210 204.4 115.7 12.4 27 A GLN N 211 202.7 115.9 13.9 29 A GLN CA 211 202.1 114.7 13.4 32 A GLN CB 211 201.0 114.2 14.4 35 A GLN CG 211 200.4 112.9 14.2 38 A GLN CD 211 200.0 112.2 15.5 40 A GLN OE1 211 199.5 112.8 16.4 42 A GLN NE2 211 200.3 110.9 15.6 41 A GLN C 211 201.4 114.8 12.1 33 A GLN O 211 201.5 113.9 11.3 34 A GLU N 212 200.8 116.0 11.8 35 A GLU CA 212 200.2 116.2 10.5 37 A GLU CB 212 199.4 117.5 10.6 40 A GLU CG 212 198.1 117.2 11.3 45 A GLU CD 212 197.3 116.0 10.7 48 A GLU OE1 212 196.8 116.2 9.6 49 A GLU OE2 212 197.4 115.0 11.4 48 A GLU C 212 201.2 116.4 9.3 37 A GLU O 212 200.9 115.8 8.2 38 A PHE N 213 202.2 117.1 9.6 36 A PHE CA 213 203.2 117.4 8.6 34 A PHE CB 213 203.6 118.9 8.6 31 A PHE CG 213 202.4 119.8 8.3 31 A PHE CD1 213 201.5 120.1 9.4 30 A PHE CD2 213 202.1 120.2 7.1 30 A PHE CE1 213 200.4 120.8 9.1 30 A PHE CE2 213 200.9 120.9 6.8 30 A PHE CZ 213 200.0 121.2 7.8 30 A PHE C 213 204.5 116.6 8.7 35 A PHE O 213 205.5 116.9 8.1 37 A ARG N 214 204.4 115.5 9.5 36 A ARG CA 214 205.5 114.6 9.7 37 A ARG CB 214 205.7 113.7 8.5 40 A ARG CG 214 204.7 112.6 8.5 45 A ARG CD 214 204.1 112.3 7.1 49 A ARG NE 214 202.7 112.6 7.1 54 A ARG CZ 214 201.7 111.8 7.5 57 A ARG NH1 214 200.4 112.2 7.5 57 A ARG NH2 214 201.9 110.6 7.9 59 A ARG C 214 206.8 115.4 10.0 36 A ARG O 214 207.9 115.1 9.3 36 A LEU N 215 206.8 116.4 10.8 34 A LEU CA 215 208.0 117.1 11.2 32 A LEU CB 215 207.7 118.6 11.3 32 A LEU CG 215 206.9 119.3 10.2 32 A LEU CD1 215 206.8 120.8 10.6 33 A LEU CD2 215 207.6 119.2 8.9 33 A LEU C 215 208.7 116.6 12.4 32 A LEU O 215 209.0 117.3 13.3 32 A TRP N 216 209.1 115.3 12.4 33 A TRP CA 216 209.7 114.6 13.5 33 A TRP CB 216 209.5 113.1 13.4 31 A TRP CG 216 208.1 112.7 13.3 30 A TRP CD2 216 207.1 112.6 14.4 29 A TRP CE2 216 205.9 112.3 13.9 29 A TRP CE3 216 207.2 112.8 15.8 29 A TRP CD1 216 207.3 112.5 12.2 30 A TRP NE1 216 206.0 112.2 12.5 29 A TRP CZ2 216 204.7 112.1 14.7 28 A TRP CZ3 216 206.1 112.6 16.6 27 A TRP CH2 216 204.9 112.3 16.0 27 A TRP C 216 211.2 114.8 13.7 35 A TRP O 216 211.7 114.9 14.9 37 A ASP N 217 212.0 114.9 12.6 37 A ASP CA 217 213.4 115.1 12.7 38 A ASP CB 217 214.0 115.5 11.4 39 A ASP CG 217 213.5 114.5 10.3 41 A ASP OD1 217 213.5 115.0 9.1 43 A ASP OD2 217 213.1 113.4 10.6 41 A ASP C 217 214.2 115.8 13.8 38 A ASP O 217 215.1 115.2 14.4 38 A ASN N 218 213.8 117.0 14.2 38 A ASN CA 218 214.5 117.7 15.2 38 A ASN CB 218 215.0 119.0 14.8 40 A ASN CG 218 215.6 119.0 13.4 42 A ASN OD1 218 214.9 119.2 12.4 44 A ASN ND2 218 216.9 118.6 13.3 43 A ASN C 218 213.8 117.8 16.6 35 A ASN O 218 214.2 118.6 17.4 35 A GLU N 219 212.7 117.1 16.7 34 A GLU CA 219 211.9 117.3 18.0 33 A GLU CB 219 210.5 116.8 17.8 32 A GLU CG 219 209.6 117.2 19.0 31 A GLU CD 219 209.4 118.7 19.2 31 A GLU OE1 219 210.0 119.5 18.4 30 A GLU OE2 219 208.7 119.1 20.1 29 A GLU C 219 212.6 116.7 19.2 32 A GLU O 219 212.5 117.3 20.3 31 A LEU N 220 213.3 115.5 19.1 33 A LEU CA 220 213.9 114.9 20.3 32 A LEU CB 220 214.4 113.5 20.0 32 A LEU CG 220 214.7 112.7 21.3 32 A LEU CD1 220 213.5 112.7 22.2 33 A LEU CD2 220 215.1 111.3 20.9 31 A LEU C 220 215.1 115.8 20.7 33 A LEU O 220 215.4 115.9 21.9 34 A GLN N 221 215.6 116.6 19.8 34 A GLN CA 221 216.7 117.5 20.1 35 A GLN CB 221 217.4 117.9 18.8 39 A GLN CG 221 218.4 119.0 18.9 44 A GLN CD 221 219.0 119.4 17.5 47 A GLN OE1 221 219.5 118.6 16.8 48 A GLN NE2 221 218.8 120.7 17.2 49 A GLN C 221 216.2 118.7 20.8 34 A GLN O 221 216.9 119.3 21.7 34 A TYR N 222 215.0 119.1 20.4 32 A TYR CA 222 214.3 120.2 21.1 30 A TYR CB 222 213.1 120.6 20.3 28 A TYR CG 222 212.4 121.8 20.9 27 A TYR CD1 222 213.0 123.0 21.0 26 A TYR CE1 222 212.3 124.1 21.5 26 A TYR CD2 222 211.1 121.7 21.4 27 A TYR CE2 222 210.4 122.7 22.0 26 A TYR CZ 222 211.0 124.0 22.0 27 A TYR OH 222 210.4 125.0 22.6 26 A TYR C 222 214.0 119.8 22.5 31 A TYR O 222 214.2 120.6 23.5 31 A VAL N 223 213.5 118.6 22.7 32 A VAL CA 223 213.1 118.0 24.0 32 A VAL CB 223 212.5 116.6 23.8 31 A VAL CG1 223 212.7 115.8 25.1 30 A VAL CG2 223 211.0 116.8 23.5 30 A VAL C 223 214.4 118.0 24.9 32 A VAL O 223 214.3 118.3 26.1 34 A ASP N 224 215.5 117.5 24.4 33 A ASP CA 224 216.7 117.5 25.1 34 A ASP CB 224 217.8 116.8 24.4 34 A ASP CG 224 217.7 115.4 24.2 34 A ASP OD1 224 217.0 114.7 25.1 34 A ASP OD2 224 218.1 114.8 23.2 34 A ASP C 224 217.1 118.9 25.6 35 A ASP O 224 217.7 119.1 26.7 35 A GLN N 225 216.9 119.9 24.8 35 A GLN CA 225 217.2 121.2 25.1 35 A GLN CB 225 216.9 122.2 23.9 37 A GLN CG 225 217.0 123.6 24.2 40 A GLN CD 225 216.3 124.5 23.1 43 A GLN OE1 225 216.4 124.2 21.9 44 A GLN NE2 225 215.7 125.6 23.5 43 A GLN C 225 216.3 121.7 26.3 34 A GLN O 225 216.8 122.2 27.3 34 A LEU N 226 215.0 121.5 26.2 33 A LEU CA 226 214.1 121.9 27.3 32 A LEU CB 226 212.6 121.9 26.8 31 A LEU CG 226 212.2 122.8 25.7 31 A LEU CD1 226 210.8 123.3 25.9 30 A LEU CD2 226 213.1 124.1 25.8 31 A LEU C 226 214.3 121.1 28.6 33 A LEU O 226 214.1 121.7 29.7 32 A LEU N 227 214.6 119.8 28.5 34 A LEU CA 227 214.8 119.0 29.7 35 A LEU CB 227 215.0 117.5 29.4 34 A LEU CG 227 213.7 116.8 29.2 34 A LEU CD1 227 214.0 115.3 28.7 33 A LEU CD2 227 212.8 116.8 30.4 32 A LEU C 227 216.1 119.5 30.5 36 A LEU O 227 216.1 119.5 31.7 36 A LYS N 228 217.0 120.1 29.7 37 A LYS CA 228 218.2 120.6 30.2 37 A LYS CB 228 219.2 120.8 29.1 39 A LYS CG 228 220.6 121.1 29.4 43 A LYS CD 228 221.5 120.9 28.2 46 A LYS CE 228 222.9 121.4 28.4 49 A LYS NZ 228 223.7 121.3 27.2 50 A LYS C 228 217.9 121.9 31.0 37 A LYS O 228 218.6 122.2 32.0 37 A GLU N 229 217.0 122.7 30.5 35 A GLU CA 229 216.6 123.9 31.1 33 A GLU CB 229 215.8 124.8 30.1 33 A GLU CG 229 216.5 125.0 28.8 34 A GLU CD 229 215.9 126.0 27.9 34 A GLU OE1 229 214.7 126.2 28.0 35 A GLU OE2 229 216.6 126.5 27.1 36 A GLU C 229 215.8 123.7 32.4 32 A GLU O 229 215.8 124.4 33.3 32 A ASP N 230 215.0 122.6 32.3 31 A ASP CA 230 214.1 122.3 33.5 30 A ASP CB 230 212.9 123.2 33.6 29 A ASP CG 230 212.2 123.0 34.9 29 A ASP OD1 230 212.6 122.1 35.7 30 A ASP OD2 230 211.2 123.8 35.1 29 A ASP C 230 213.7 120.8 33.4 30 A ASP O 230 212.7 120.5 32.8 31 A VAL N 231 214.6 120.0 34.0 30 A VAL CA 231 214.3 118.5 34.0 30 A VAL CB 231 215.6 117.7 34.6 31 A VAL CG1 231 215.6 117.9 36.1 31 A VAL CG2 231 215.5 116.3 34.1 30 A VAL C 231 213.0 118.1 34.7 30 A VAL O 231 212.6 117.0 34.6 31 A ARG N 232 212.4 119.1 35.3 30 A ARG CA 232 211.2 118.8 36.0 30 A ARG CB 232 211.1 119.6 37.3 30 A ARG CG 232 212.2 119.4 38.3 31 A ARG CD 232 211.8 120.1 39.7 32 A ARG NE 232 212.7 119.7 40.8 34 A ARG CZ 232 213.9 120.3 41.0 35 A ARG NH1 232 214.3 121.3 40.2 35 A ARG NH2 232 214.7 120.0 42.0 35 A ARG C 232 210.0 119.2 35.1 28 A ARG O 232 208.8 119.2 35.5 28 A ASN N 233 210.2 119.5 33.8 26 A ASN CA 233 209.1 119.9 33.0 25 A ASN CB 233 209.6 120.8 31.8 25 A ASN CG 233 208.4 121.4 31.0 25 A ASN OD1 233 207.3 120.9 31.0 27 A ASN ND2 233 208.7 122.5 30.4 24 A ASN C 233 208.4 118.7 32.5 25 A ASN O 233 208.9 118.0 31.5 27 A ASN N 234 207.3 118.4 33.0 26 A ASN CA 234 206.5 117.3 32.7 25 A ASN CB 234 205.3 117.1 33.6 26 A ASN CG 234 204.9 115.7 33.7 25 A ASN OD1 234 205.6 114.8 34.0 25 A ASN ND2 234 203.6 115.5 33.5 26 A ASN C 234 206.0 117.3 31.2 25 A ASN O 234 205.8 116.3 30.6 25 A SER N 235 205.7 118.5 30.7 23 A SER CA 235 205.3 118.7 29.3 21 A SER CB 235 205.0 120.2 29.1 19 A SER OG 235 203.9 120.6 29.9 17 A SER C 235 206.3 118.2 28.3 21 A SER O 235 206.0 117.7 27.3 20 A VAL N 236 207.6 118.3 28.7 22 A VAL CA 236 208.7 117.9 27.9 22 A VAL CB 236 209.9 118.7 28.3 21 A VAL CG1 236 211.1 118.3 27.3 22 A VAL CG2 236 209.7 120.1 28.2 20 A VAL C 236 208.9 116.4 28.0 23 A VAL O 236 209.3 115.8 27.1 25 A TRP N 237 208.7 115.8 29.2 24 A TRP CA 237 208.8 114.4 29.3 26 A TRP CB 237 208.7 113.9 30.8 26 A TRP CG 237 209.9 114.2 31.6 26 A TRP CD2 237 211.1 113.4 31.6 26 A TRP CE2 237 212.0 114.0 32.5 25 A TRP CE3 237 211.5 112.2 31.0 25 A TRP CD1 237 210.2 115.3 32.4 25 A TRP NE1 237 211.4 115.2 32.9 26 A TRP CZ2 237 213.3 113.5 32.8 24 A TRP CZ3 237 212.8 111.7 31.3 24 A TRP CH2 237 213.6 112.3 32.1 24 A TRP C 237 207.7 113.8 28.5 26 A TRP O 237 207.9 112.8 27.8 26 A ASN N 238 206.5 114.5 28.5 25 A ASN CA 238 205.4 114.0 27.7 24 A ASN CB 238 204.2 114.8 27.9 24 A ASN CG 238 203.0 114.3 27.1 25 A ASN OD1 238 202.6 113.2 27.3 25 A ASN ND2 238 202.5 115.1 26.2 24 A ASN C 238 205.8 114.0 26.2 23 A ASN O 238 205.6 113.1 25.5 24 A GLN N 239 206.4 115.1 25.8 23 A GLN CA 239 206.9 115.3 24.4 23 A GLN CB 239 207.4 116.7 24.1 23 A GLN CG 239 207.6 117.1 22.7 23 A GLN CD 239 206.2 117.3 21.9 24 A GLN OE1 239 205.2 116.8 22.4 25 A GLN NE2 239 206.3 117.9 20.8 23 A GLN C 239 207.9 114.3 24.0 24 A GLN O 239 207.9 113.9 22.8 24 A ARG N 240 208.8 113.9 24.9 25 A ARG CA 240 209.8 113.0 24.7 25 A ARG CB 240 210.7 112.8 25.9 25 A ARG CG 240 211.9 111.9 25.7 26 A ARG CD 240 212.7 111.7 27.0 26 A ARG NE 240 214.0 111.2 26.6 27 A ARG CZ 240 215.0 111.9 26.0 29 A ARG NH1 240 214.7 113.2 25.8 30 A ARG NH2 240 216.0 111.4 25.5 30 A ARG C 240 209.2 111.6 24.3 26 A ARG O 240 209.6 111.0 23.4 30 A HIS N 241 208.2 111.2 25.1 26 A HIS CA 241 207.4 110.0 24.9 24 A HIS CB 241 206.5 109.7 26.0 24 A HIS CG 241 205.9 108.4 26.0 24 A HIS CD2 241 206.2 107.2 26.6 24 A HIS ND1 241 204.8 108.1 25.3 23 A HIS CE1 241 204.4 106.8 25.4 24 A HIS NE2 241 205.3 106.3 26.3 24 A HIS C 241 206.7 110.0 23.6 24 A HIS O 241 206.7 109.1 22.8 25 A PHE N 242 206.0 111.2 23.3 24 A PHE CA 242 205.2 111.3 22.0 23 A PHE CB 242 204.6 112.7 22.0 22 A PHE CG 242 203.9 113.0 20.7 22 A PHE CD1 242 202.7 112.5 20.4 21 A PHE CD2 242 204.4 114.0 19.8 22 A PHE CE1 242 202.0 112.9 19.2 21 A PHE CE2 242 203.8 114.4 18.7 22 A PHE CZ 242 202.5 113.8 18.4 21 A PHE C 242 206.2 111.2 20.8 24 A PHE O 242 205.8 110.5 19.9 24 A VAL N 243 207.3 111.8 20.9 25 A VAL CA 243 208.3 111.7 19.8 27 A VAL CB 243 209.5 112.7 20.0 27 A VAL CG1 243 210.6 112.5 19.0 26 A VAL CG2 243 208.9 114.1 20.0 27 A VAL C 243 208.8 110.3 19.6 28 A VAL O 243 208.7 109.7 18.5 28 A ILE N 244 209.3 109.7 20.7 28 A ILE CA 244 209.9 108.3 20.6 28 A ILE CB 244 210.5 107.9 21.9 27 A ILE CG2 244 211.1 106.5 21.9 27 A ILE CG1 244 211.7 108.8 22.2 25 A ILE CD1 244 212.4 108.5 23.5 23 A ILE C 244 208.8 107.4 20.2 29 A ILE O 244 209.0 106.7 19.2 29 A SER N 245 207.6 107.4 20.8 29 A SER CA 245 206.6 106.5 20.4 31 A SER CB 245 205.3 106.9 21.2 31 A SER OG 245 205.5 106.7 22.6 35 A SER C 245 206.2 106.6 19.0 33 A SER O 245 205.9 105.5 18.4 35 A ASN N 246 206.2 107.7 18.4 34 A ASN CA 246 205.8 107.8 17.0 34 A ASN CB 246 205.0 109.1 16.7 33 A ASN CG 246 203.7 109.1 17.6 32 A ASN OD1 246 203.7 109.7 18.7 32 A ASN ND2 246 202.6 108.6 17.1 32 A ASN C 246 206.9 107.7 15.9 34 A ASN O 246 206.6 107.7 14.7 34 A THR N 247 208.1 107.6 16.4 34 A THR CA 247 209.2 107.4 15.5 34 A THR CB 247 210.3 108.5 15.8 33 A THR OG1 247 210.7 108.6 17.2 33 A THR CG2 247 209.8 109.9 15.4 32 A THR C 247 209.8 106.0 15.6 35 A THR O 247 209.3 105.1 15.0 36 A THR N 248 210.7 105.8 16.6 36 A THR CA 248 211.3 104.4 16.8 36 A THR CB 248 212.7 104.6 17.4 36 A THR OG1 248 212.5 105.1 18.8 37 A THR CG2 248 213.6 105.5 16.7 36 A THR C 248 210.5 103.5 17.6 37 A THR O 248 210.5 102.3 17.4 39 A GLY N 249 209.9 104.0 18.7 38 A GLY CA 249 209.1 103.1 19.6 37 A GLY C 249 210.1 102.7 20.7 38 A GLY O 249 211.3 103.0 20.6 37 A TYR N 250 209.6 102.0 21.7 40 A TYR CA 250 210.4 101.5 22.8 42 A TYR CB 250 209.8 101.8 24.1 41 A TYR CG 250 209.7 103.3 24.4 41 A TYR CD1 250 208.7 104.1 23.8 40 A TYR CE1 250 208.5 105.4 24.1 40 A TYR CD2 250 210.5 103.9 25.3 40 A TYR CE2 250 210.4 105.2 25.7 41 A TYR CZ 250 209.4 106.0 25.1 40 A TYR OH 250 209.2 107.3 25.4 40 A TYR C 250 210.7 100.0 22.7 44 A TYR O 250 211.1 99.4 23.7 44 A SER N 251 210.3 99.4 21.6 46 A SER CA 251 210.6 98.0 21.4 48 A SER CB 251 209.7 97.5 20.2 49 A SER OG 251 208.4 97.6 20.5 51 A SER C 251 212.0 97.7 21.1 49 A SER O 251 212.6 96.7 21.5 50 A ASP N 252 212.6 98.7 20.4 51 A ASP CA 252 214.1 98.7 20.2 52 A ASP CB 252 214.5 99.9 19.3 55 A ASP CG 252 215.9 99.8 18.8 57 A ASP OD1 252 216.6 98.8 19.0 59 A ASP OD2 252 216.3 100.8 18.1 58 A ASP C 252 214.8 98.7 21.5 52 A ASP O 252 214.7 99.7 22.2 51 A ARG N 253 215.4 97.5 21.9 52 A ARG CA 253 216.1 97.4 23.1 51 A ARG CB 253 216.8 96.0 23.1 54 A ARG CG 253 215.9 94.8 23.2 58 A ARG CD 253 216.8 93.5 22.9 60 A ARG NE 253 216.0 92.3 23.2 62 A ARG CZ 253 216.3 91.1 22.6 63 A ARG NH1 253 217.2 91.0 21.6 62 A ARG NH2 253 215.6 90.1 22.9 63 A ARG C 253 217.2 98.4 23.3 49 A ARG O 253 217.6 98.8 24.4 48 A ALA N 254 217.7 98.9 22.1 47 A ALA CA 254 218.7 100.0 22.2 45 A ALA CB 254 219.4 100.0 20.8 45 A ALA C 254 218.1 101.3 22.5 43 A ALA O 254 218.7 102.1 23.3 43 A VAL N 255 217.0 101.6 22.0 43 A VAL CA 255 216.3 102.9 22.3 42 A VAL CB 255 215.1 103.1 21.4 42 A VAL CG1 255 214.3 104.3 21.9 42 A VAL CG2 255 215.5 103.3 20.0 42 A VAL C 255 215.8 102.8 23.8 42 A VAL O 255 216.0 103.7 24.5 43 A LEU N 256 215.3 101.6 24.1 42 A LEU CA 256 214.8 101.3 25.5 42 A LEU CB 256 214.3 99.9 25.6 41 A LEU CG 256 213.6 99.4 26.8 41 A LEU CD1 256 212.3 100.2 27.2 40 A LEU CD2 256 213.2 98.0 26.5 41 A LEU C 256 216.0 101.5 26.5 44 A LEU O 256 215.9 102.3 27.4 44 A GLU N 257 217.1 100.9 26.2 45 A GLU CA 257 218.3 101.0 27.1 46 A GLU CB 257 219.4 100.1 26.5 48 A GLU CG 257 220.8 100.4 27.1 51 A GLU CD 257 220.9 99.7 28.5 54 A GLU OE1 257 220.3 100.1 29.5 54 A GLU OE2 257 221.8 98.8 28.6 56 A GLU C 257 218.7 102.5 27.2 44 A GLU O 257 218.9 102.9 28.4 44 A ARG N 258 218.8 103.1 26.1 44 A ARG CA 258 219.2 104.5 26.1 43 A ARG CB 258 219.1 105.1 24.6 42 A ARG CG 258 219.6 106.5 24.5 43 A ARG CD 258 219.1 107.2 23.2 43 A ARG NE 258 217.7 107.4 23.2 44 A ARG CZ 258 217.0 107.4 22.1 44 A ARG NH1 258 217.5 107.2 20.9 44 A ARG NH2 258 215.6 107.5 22.1 44 A ARG C 258 218.4 105.4 27.0 42 A ARG O 258 218.8 106.3 27.7 43 A GLU N 259 217.0 105.2 26.9 41 A GLU CA 259 216.0 105.9 27.6 40 A GLU CB 259 214.6 105.6 27.1 40 A GLU CG 259 214.4 106.3 25.7 40 A GLU CD 259 214.6 107.8 25.7 40 A GLU OE1 259 213.9 108.5 26.5 40 A GLU OE2 259 215.5 108.3 25.0 38 A GLU C 259 216.1 105.6 29.1 39 A GLU O 259 216.0 106.5 29.9 39 A VAL N 260 216.1 104.3 29.4 40 A VAL CA 260 216.2 103.8 30.8 41 A VAL CB 260 216.0 102.3 30.9 41 A VAL CG1 260 216.3 101.8 32.3 41 A VAL CG2 260 214.6 101.9 30.5 41 A VAL C 260 217.4 104.3 31.5 42 A VAL O 260 217.4 104.8 32.6 42 A GLN N 261 218.5 104.2 30.8 43 A GLN CA 261 219.8 104.7 31.3 44 A GLN CB 261 220.9 104.4 30.4 47 A GLN CG 261 222.3 104.2 31.1 51 A GLN CD 261 222.5 102.8 31.7 52 A GLN OE1 261 222.4 101.8 31.0 53 A GLN NE2 261 222.7 102.8 33.1 53 A GLN C 261 219.7 106.2 31.6 43 A GLN O 261 220.0 106.7 32.7 44 A TYR N 262 219.4 107.0 30.5 42 A TYR CA 262 219.2 108.4 30.6 40 A TYR CB 262 218.6 109.0 29.3 40 A TYR CG 262 218.1 110.4 29.5 40 A TYR CD1 262 219.0 111.4 29.6 40 A TYR CE1 262 218.5 112.7 29.8 39 A TYR CD2 262 216.7 110.7 29.6 40 A TYR CE2 262 216.3 112.0 29.8 39 A TYR CZ 262 217.2 113.0 29.8 39 A TYR OH 262 216.8 114.3 30.0 38 A TYR C 262 218.4 108.9 31.8 39 A TYR O 262 218.7 109.8 32.5 40 A THR N 263 217.2 108.2 31.9 39 A THR CA 263 216.2 108.5 32.9 39 A THR CB 263 214.9 107.7 32.7 38 A THR OG1 263 214.5 107.9 31.4 37 A THR CG2 263 213.8 108.2 33.6 37 A THR C 263 216.8 108.2 34.3 40 A THR O 263 216.7 109.0 35.2 41 A LEU N 264 217.4 107.0 34.5 41 A LEU CA 264 218.1 106.7 35.7 43 A LEU CB 264 218.7 105.3 35.6 43 A LEU CG 264 217.8 104.1 35.6 42 A LEU CD1 264 218.7 102.8 35.4 42 A LEU CD2 264 217.0 103.9 36.9 42 A LEU C 264 219.1 107.7 36.1 44 A LEU O 264 219.2 108.2 37.2 44 A GLU N 265 219.9 108.2 35.1 46 A GLU CA 265 220.9 109.2 35.3 48 A GLU CB 265 221.7 109.5 34.0 50 A GLU CG 265 222.2 108.3 33.3 54 A GLU CD 265 223.0 107.4 34.2 57 A GLU OE1 265 222.5 106.3 34.7 57 A GLU OE2 265 224.2 107.7 34.4 58 A GLU C 265 220.2 110.5 35.8 48 A GLU O 265 220.7 111.1 36.7 49 A MET N 266 219.0 110.8 35.3 47 A MET CA 266 218.3 112.0 35.7 45 A MET CB 266 217.1 112.3 34.7 44 A MET CG 266 217.5 112.6 33.3 44 A MET SD 266 219.0 113.6 33.3 44 A MET CE 266 218.3 115.1 32.9 45 A MET C 266 217.8 111.8 37.1 45 A MET O 266 217.7 112.8 37.8 45 A ILE N 267 217.4 110.6 37.4 45 A ILE CA 267 216.9 110.3 38.7 46 A ILE CB 267 216.4 108.8 38.8 45 A ILE CG2 267 216.0 108.5 40.2 45 A ILE CG1 267 215.2 108.7 37.9 44 A ILE CD1 267 214.7 107.3 37.7 44 A ILE C 267 218.0 110.5 39.8 47 A ILE O 267 217.9 111.2 40.8 47 A LYS N 268 219.2 109.9 39.5 48 A LYS CA 268 220.3 110.1 40.3 50 A LYS CB 268 221.6 109.5 39.7 52 A LYS CG 268 221.4 108.0 39.5 56 A LYS CD 268 222.5 107.3 38.7 59 A LYS CE 268 222.2 105.9 38.2 61 A LYS NZ 268 223.3 105.2 37.6 62 A LYS C 268 220.6 111.5 40.7 50 A LYS O 268 220.7 111.9 41.8 51 A LEU N 269 220.5 112.4 39.7 50 A LEU CA 269 220.6 113.9 39.9 48 A LEU CB 269 220.8 114.6 38.5 48 A LEU CG 269 221.8 114.2 37.5 48 A LEU CD1 269 222.2 115.5 36.7 48 A LEU CD2 269 223.0 113.6 38.0 49 A LEU C 269 219.6 114.6 40.7 47 A LEU O 269 219.9 115.4 41.6 48 A VAL N 270 218.3 114.3 40.3 44 A VAL CA 270 217.2 115.0 41.1 43 A VAL CB 270 216.5 116.1 40.2 41 A VAL CG1 270 215.6 117.0 41.0 39 A VAL CG2 270 217.5 116.9 39.4 39 A VAL C 270 216.2 113.9 41.5 43 A VAL O 270 215.1 113.8 41.0 43 A PRO N 271 216.7 113.1 42.5 44 A PRO CD 271 217.9 113.3 43.3 44 A PRO CA 271 215.9 112.0 43.2 44 A PRO CB 271 216.8 111.8 44.4 44 A PRO CG 271 218.1 112.0 44.0 44 A PRO C 271 214.5 112.2 43.5 44 A PRO O 271 213.7 111.3 43.6 44 A HIS N 272 214.1 113.5 43.8 44 A HIS CA 272 212.7 113.8 44.2 43 A HIS CB 272 212.7 114.7 45.4 45 A HIS CG 272 213.2 114.1 46.6 46 A HIS CD2 272 214.4 113.9 47.2 46 A HIS ND1 272 212.3 113.4 47.5 47 A HIS CE1 272 213.0 112.9 48.5 47 A HIS NE2 272 214.3 113.2 48.3 47 A HIS C 272 211.9 114.4 43.0 42 A HIS O 272 210.8 114.9 43.3 42 A ASN N 273 212.4 114.3 41.8 39 A ASN CA 273 211.7 114.8 40.6 37 A ASN CB 273 212.7 115.2 39.5 35 A ASN CG 273 212.0 115.5 38.2 33 A ASN OD1 273 210.8 116.0 38.2 32 A ASN ND2 273 212.7 115.4 37.1 32 A ASN C 273 210.9 113.7 40.2 35 A ASN O 273 211.3 112.7 39.6 35 A GLU N 274 209.6 113.8 40.4 35 A GLU CA 274 208.6 112.8 40.0 34 A GLU CB 274 207.2 113.2 40.5 35 A GLU CG 274 206.2 112.2 40.3 37 A GLU CD 274 204.9 112.6 40.8 39 A GLU OE1 274 203.9 112.2 40.3 41 A GLU OE2 274 204.9 113.4 41.8 41 A GLU C 274 208.5 112.5 38.5 34 A GLU O 274 208.2 111.4 38.1 35 A SER N 275 208.8 113.5 37.7 33 A SER CA 275 208.6 113.3 36.2 31 A SER CB 275 208.9 114.6 35.4 31 A SER OG 275 207.8 115.5 35.6 31 A SER C 275 209.5 112.2 35.7 32 A SER O 275 209.1 111.4 34.9 31 A ALA N 276 210.8 112.2 36.1 32 A ALA CA 276 211.7 111.2 35.6 32 A ALA CB 276 213.1 111.5 36.0 32 A ALA C 276 211.2 109.8 36.1 32 A ALA O 276 211.3 108.8 35.4 32 A TRP N 277 210.6 109.8 37.3 33 A TRP CA 277 210.1 108.6 37.9 34 A TRP CB 277 209.7 108.8 39.3 35 A TRP CG 277 210.9 108.7 40.2 37 A TRP CD2 277 211.6 107.5 40.6 38 A TRP CE2 277 212.7 107.9 41.4 38 A TRP CE3 277 211.5 106.1 40.3 37 A TRP CD1 277 211.6 109.7 40.8 38 A TRP NE1 277 212.6 109.3 41.6 39 A TRP CZ2 277 213.6 107.0 42.0 38 A TRP CZ3 277 212.4 105.2 40.9 37 A TRP CH2 277 213.4 105.6 41.7 37 A TRP C 277 208.9 108.0 37.1 33 A TRP O 277 208.8 106.9 36.9 33 A ASN N 278 208.0 108.9 36.8 34 A ASN CA 278 206.8 108.6 36.1 34 A ASN CB 278 205.8 109.8 36.1 34 A ASN CG 278 205.2 110.1 37.4 35 A ASN OD1 278 205.5 109.4 38.4 35 A ASN ND2 278 204.5 111.2 37.5 36 A ASN C 278 207.1 108.1 34.7 33 A ASN O 278 206.3 107.3 34.1 33 A TYR N 279 208.2 108.7 34.1 32 A TYR CA 279 208.6 108.3 32.8 31 A TYR CB 279 209.5 109.4 32.2 31 A TYR CG 279 210.0 109.1 30.8 31 A TYR CD1 279 209.1 109.3 29.7 30 A TYR CE1 279 209.5 109.0 28.4 30 A TYR CD2 279 211.3 108.7 30.5 30 A TYR CE2 279 211.7 108.4 29.2 31 A TYR CZ 279 210.8 108.6 28.2 30 A TYR OH 279 211.3 108.4 26.9 31 A TYR C 279 209.3 106.9 32.8 32 A TYR O 279 209.0 106.1 31.9 33 A LEU N 280 210.1 106.7 33.9 33 A LEU CA 280 210.8 105.4 34.0 33 A LEU CB 280 211.6 105.3 35.3 33 A LEU CG 280 212.4 104.1 35.6 33 A LEU CD1 280 213.4 103.8 34.4 32 A LEU CD2 280 213.1 104.2 36.9 32 A LEU C 280 209.7 104.2 34.1 34 A LEU O 280 209.8 103.2 33.4 33 A LYS N 281 208.7 104.5 34.9 35 A LYS CA 281 207.7 103.5 35.1 37 A LYS CB 281 206.8 103.9 36.2 38 A LYS CG 281 205.7 102.9 36.6 40 A LYS CD 281 205.1 103.2 37.9 42 A LYS CE 281 204.3 104.5 37.8 44 A LYS NZ 281 204.2 105.2 39.2 44 A LYS C 281 206.9 103.4 33.8 38 A LYS O 281 206.7 102.3 33.3 39 A GLY N 282 206.5 104.6 33.2 38 A GLY CA 282 205.8 104.6 32.0 37 A GLY C 282 206.3 103.8 30.8 38 A GLY O 282 205.6 103.3 30.1 39 A ILE N 283 207.7 103.8 30.6 39 A ILE CA 283 208.2 103.1 29.5 40 A ILE CB 283 209.5 103.8 29.0 39 A ILE CG2 283 209.2 105.2 28.6 39 A ILE CG1 283 210.6 103.8 30.0 37 A ILE CD1 283 211.9 104.4 29.6 36 A ILE C 283 208.5 101.6 29.7 42 A ILE O 283 208.7 100.8 28.8 43 A LEU N 284 208.6 101.2 31.0 46 A LEU CA 284 208.9 99.8 31.4 47 A LEU CB 284 209.8 99.6 32.5 46 A LEU CG 284 211.2 100.2 32.4 46 A LEU CD1 284 212.0 100.1 33.7 46 A LEU CD2 284 212.0 99.5 31.3 46 A LEU C 284 207.6 99.0 31.7 49 A LEU O 284 207.4 97.9 31.4 49 A GLN N 285 206.7 99.7 32.4 53 A GLN CA 285 205.4 99.2 32.9 56 A GLN CB 285 204.5 100.3 33.5 58 A GLN CG 285 203.8 101.2 32.5 59 A GLN CD 285 202.8 102.2 33.1 61 A GLN OE1 285 202.0 102.8 32.4 62 A GLN NE2 285 202.9 102.4 34.4 61 A GLN C 285 204.6 98.5 31.8 58 A GLN O 285 203.7 97.8 32.0 59 A ASP N 286 204.9 98.9 30.5 61 A ASP CA 286 204.2 98.3 29.4 63 A ASP CB 286 203.8 99.4 28.4 66 A ASP CG 286 202.3 99.7 28.3 68 A ASP OD1 286 201.8 99.5 27.1 69 A ASP OD2 286 201.7 100.0 29.3 69 A ASP C 286 204.9 97.1 28.8 64 A ASP O 286 205.2 97.1 27.7 65 A ARG N 287 205.1 96.1 29.7 63 A ARG CA 287 205.8 94.8 29.4 62 A ARG CB 287 207.1 95.0 28.7 63 A ARG CG 287 207.7 93.6 28.4 65 A ARG CD 287 209.2 93.6 28.1 67 A ARG NE 287 209.9 92.4 28.4 69 A ARG CZ 287 210.7 91.7 27.6 69 A ARG NH1 287 211.1 92.3 26.4 69 A ARG NH2 287 211.2 90.5 27.9 69 A ARG C 287 205.9 94.1 30.7 60 A ARG O 287 206.0 92.8 30.8 60 A GLY N 288 206.0 94.8 31.8 58 A GLY CA 288 206.1 94.3 33.1 55 A GLY C 288 207.4 94.6 33.7 54 A GLY O 288 208.5 94.3 33.2 55 A LEU N 289 207.4 95.3 34.9 52 A LEU CA 289 208.6 95.7 35.6 51 A LEU CB 289 208.3 96.5 36.8 50 A LEU CG 289 208.3 98.1 36.8 49 A LEU CD1 289 208.1 98.6 35.4 49 A LEU CD2 289 207.2 98.6 37.7 48 A LEU C 289 209.5 94.4 36.0 51 A LEU O 289 210.7 94.5 36.0 52 A SER N 290 208.8 93.3 36.2 51 A SER CA 290 209.4 92.1 36.6 51 A SER CB 290 208.4 91.1 37.2 51 A SER OG 290 207.4 90.8 36.3 52 A SER C 290 210.3 91.4 35.5 50 A SER O 290 211.0 90.4 35.8 49 A ARG N 291 210.1 91.8 34.2 50 A ARG CA 291 210.9 91.2 33.1 50 A ARG CB 291 210.1 91.4 31.8 52 A ARG CG 291 209.1 90.3 31.6 56 A ARG CD 291 208.4 90.5 30.3 60 A ARG NE 291 208.2 89.2 29.6 64 A ARG CZ 291 208.1 89.0 28.3 65 A ARG NH1 291 207.9 87.8 27.7 66 A ARG NH2 291 208.3 90.1 27.5 66 A ARG C 291 212.3 91.9 33.0 49 A ARG O 291 213.0 91.7 32.1 48 A TYR N 292 212.6 92.7 34.0 47 A TYR CA 292 213.8 93.4 34.2 46 A TYR CB 292 213.6 94.9 33.9 43 A TYR CG 292 212.9 95.2 32.6 42 A TYR CD1 292 211.5 95.5 32.6 41 A TYR CE1 292 210.9 95.6 31.3 41 A TYR CD2 292 213.6 95.1 31.4 41 A TYR CE2 292 213.0 95.2 30.2 40 A TYR CZ 292 211.6 95.5 30.2 40 A TYR OH 292 211.0 95.8 28.9 39 A TYR C 292 214.4 93.2 35.6 46 A TYR O 292 214.2 93.9 36.5 46 A PRO N 293 215.1 92.0 35.7 47 A PRO CD 293 215.3 91.0 34.6 46 A PRO CA 293 215.7 91.6 37.0 47 A PRO CB 293 216.2 90.2 36.6 46 A PRO CG 293 216.5 90.3 35.2 45 A PRO C 293 216.7 92.5 37.6 48 A PRO O 293 216.7 92.6 38.8 50 A ASN N 294 217.6 93.1 36.8 49 A ASN CA 294 218.7 94.0 37.4 50 A ASN CB 294 219.6 94.4 36.3 48 A ASN CG 294 220.2 93.2 35.5 47 A ASN OD1 294 220.1 93.1 34.3 47 A ASN ND2 294 220.8 92.3 36.3 47 A ASN C 294 218.1 95.2 38.0 52 A ASN O 294 218.5 95.7 39.0 52 A LEU N 295 217.0 95.7 37.3 54 A LEU CA 295 216.3 96.9 37.7 55 A LEU CB 295 215.0 97.0 37.0 56 A LEU CG 295 214.2 98.3 36.9 56 A LEU CD1 295 215.0 99.3 36.0 56 A LEU CD2 295 212.8 98.0 36.4 56 A LEU C 295 216.2 97.0 39.3 56 A LEU O 295 216.6 98.0 39.9 56 A LEU N 296 215.6 96.0 39.9 56 A LEU CA 296 215.3 96.0 41.3 58 A LEU CB 296 214.7 94.7 41.8 56 A LEU CG 296 214.5 94.6 43.3 56 A LEU CD1 296 213.7 95.8 43.9 55 A LEU CD2 296 213.7 93.3 43.6 56 A LEU C 296 216.6 96.3 42.1 60 A LEU O 296 216.6 97.2 43.0 60 A ASN N 297 217.7 95.7 41.7 62 A ASN CA 297 219.0 95.9 42.4 65 A ASN CB 297 220.1 95.1 41.7 66 A ASN CG 297 219.8 93.7 41.6 68 A ASN OD1 297 218.8 93.2 42.0 69 A ASN ND2 297 220.8 92.9 41.1 68 A ASN C 297 219.3 97.4 42.3 65 A ASN O 297 219.3 98.1 43.3 65 A GLN N 298 219.6 97.9 41.1 65 A GLN CA 298 220.0 99.3 40.8 66 A GLN CB 298 219.8 99.6 39.4 67 A GLN CG 298 219.5 98.5 38.4 68 A GLN CD 298 220.7 97.7 38.0 68 A GLN OE1 298 221.1 96.8 38.8 70 A GLN NE2 298 221.1 97.8 36.8 68 A GLN C 298 219.2 100.2 41.7 67 A GLN O 298 219.8 101.2 42.3 67 A LEU N 299 217.9 100.0 41.9 67 A LEU CA 299 217.0 100.8 42.7 68 A LEU CB 299 215.5 100.6 42.4 67 A LEU CG 299 214.9 101.1 41.1 67 A LEU CD1 299 213.4 101.1 41.3 66 A LEU CD2 299 215.4 102.5 40.7 66 A LEU C 299 217.3 100.7 44.1 69 A LEU O 299 217.5 101.7 44.9 68 A LEU N 300 217.4 99.4 44.6 70 A LEU CA 300 217.6 99.1 46.0 72 A LEU CB 300 217.7 97.6 46.1 72 A LEU CG 300 216.6 96.9 46.8 72 A LEU CD1 300 215.3 97.6 46.6 72 A LEU CD2 300 216.5 95.4 46.4 72 A LEU C 300 219.0 99.7 46.4 73 A LEU O 300 219.1 100.2 47.5 73 A ASP N 301 219.9 99.8 45.4 75 A ASP CA 301 221.2 100.4 45.7 77 A ASP CB 301 222.1 100.2 44.5 78 A ASP CG 301 222.4 98.7 44.3 78 A ASP OD1 301 221.9 97.8 45.1 79 A ASP OD2 301 223.2 98.3 43.4 78 A ASP C 301 221.1 101.9 46.0 78 A ASP O 301 221.8 102.4 46.8 79 A LEU N 302 220.2 102.6 45.3 79 A LEU CA 302 220.0 104.1 45.5 79 A LEU CB 302 219.3 104.7 44.3 80 A LEU CG 302 220.1 104.8 42.9 80 A LEU CD1 302 219.3 105.7 42.0 80 A LEU CD2 302 221.5 105.3 43.1 80 A LEU C 302 219.3 104.4 46.8 79 A LEU O 302 219.3 105.5 47.3 78 A GLN N 303 218.7 103.3 47.4 79 A GLN CA 303 217.9 103.4 48.6 80 A GLN CB 303 217.7 102.1 49.3 79 A GLN CG 303 216.4 101.4 48.9 79 A GLN CD 303 215.3 102.1 49.6 80 A GLN OE1 303 215.1 103.3 49.6 80 A GLN NE2 303 214.4 101.3 50.2 80 A GLN C 303 218.6 104.4 49.7 81 A GLN O 303 217.9 105.1 50.4 81 A PRO N 304 219.9 104.3 49.8 81 A PRO CD 304 220.8 103.1 49.5 81 A PRO CA 304 220.6 105.2 50.8 81 A PRO CB 304 221.8 104.3 51.3 81 A PRO CG 304 222.1 103.6 50.0 81 A PRO C 304 221.0 106.6 50.3 81 A PRO O 304 220.6 107.6 51.0 81 A SER N 305 221.7 106.6 49.2 81 A SER CA 305 222.2 107.9 48.7 81 A SER CB 305 223.6 107.7 48.0 80 A SER OG 305 223.6 106.6 47.2 80 A SER C 305 221.3 108.7 47.7 80 A SER O 305 221.5 109.9 47.6 80 A HIS N 306 220.3 108.1 47.1 80 A HIS CA 306 219.4 108.8 46.2 79 A HIS CB 306 219.8 108.5 44.7 80 A HIS CG 306 221.1 109.0 44.3 82 A HIS CD2 306 221.9 108.6 43.2 82 A HIS ND1 306 221.9 109.9 45.0 82 A HIS CE1 306 223.0 110.1 44.4 83 A HIS NE2 306 223.1 109.4 43.3 83 A HIS C 306 218.0 108.4 46.5 77 A HIS O 306 217.3 108.0 45.6 77 A SER N 307 217.7 108.4 47.7 75 A SER CA 307 216.3 108.0 48.2 73 A SER CB 307 216.4 107.6 49.6 74 A SER OG 307 215.2 107.0 50.0 75 A SER C 307 215.3 109.1 48.0 72 A SER O 307 215.6 110.3 48.0 73 A SER N 308 214.0 108.7 47.9 70 A SER CA 308 212.9 109.6 47.7 68 A SER CB 308 212.9 110.2 46.3 68 A SER OG 308 212.6 109.3 45.3 68 A SER C 308 211.7 108.7 47.8 65 A SER O 308 211.8 107.5 47.5 65 A PRO N 309 210.5 109.2 48.3 63 A PRO CD 309 210.2 110.6 48.7 63 A PRO CA 309 209.4 108.3 48.4 61 A PRO CB 309 208.3 109.2 49.0 62 A PRO CG 309 208.7 110.6 48.5 62 A PRO C 309 209.0 107.7 47.1 60 A PRO O 309 208.1 106.8 47.0 61 A TYR N 310 209.6 108.2 46.0 57 A TYR CA 310 209.3 107.7 44.6 55 A TYR CB 310 209.9 108.7 43.6 55 A TYR CG 310 209.4 110.1 43.9 55 A TYR CD1 310 210.2 111.0 44.5 56 A TYR CE1 310 209.6 112.3 44.8 56 A TYR CD2 310 208.0 110.4 43.6 55 A TYR CE2 310 207.5 111.6 43.9 56 A TYR CZ 310 208.3 112.5 44.6 57 A TYR OH 310 207.8 113.7 45.0 58 A TYR C 310 210.0 106.3 44.5 53 A TYR O 310 209.5 105.4 43.8 52 A LEU N 311 211.2 106.2 45.0 50 A LEU CA 311 212.0 105.0 44.9 49 A LEU CB 311 213.3 105.2 45.7 48 A LEU CG 311 214.3 104.1 45.7 48 A LEU CD1 311 214.7 103.7 44.3 48 A LEU CD2 311 215.6 104.6 46.4 48 A LEU C 311 211.2 103.9 45.7 47 A LEU O 311 210.9 102.8 45.1 46 A ILE N 312 210.7 104.2 46.9 46 A ILE CA 312 209.9 103.3 47.7 46 A ILE CB 312 209.4 104.0 49.0 46 A ILE CG2 312 208.8 102.9 49.9 46 A ILE CG1 312 210.6 104.6 49.8 47 A ILE CD1 312 211.6 103.6 50.3 46 A ILE C 312 208.7 102.9 46.9 46 A ILE O 312 208.4 101.7 46.9 48 A ALA N 313 208.0 103.8 46.2 45 A ALA CA 313 206.8 103.4 45.5 43 A ALA CB 313 206.0 104.6 45.1 43 A ALA C 313 207.2 102.5 44.2 42 A ALA O 313 206.4 101.6 43.9 41 A PHE N 314 208.3 102.8 43.6 41 A PHE CA 314 208.7 102.0 42.5 40 A PHE CB 314 209.9 102.6 41.8 40 A PHE CG 314 210.0 102.4 40.3 40 A PHE CD1 314 209.8 103.5 39.4 41 A PHE CD2 314 210.3 101.2 39.8 40 A PHE CE1 314 209.8 103.3 38.0 41 A PHE CE2 314 210.4 101.0 38.4 40 A PHE CZ 314 210.1 102.0 37.5 41 A PHE C 314 208.9 100.6 42.8 41 A PHE O 314 208.6 99.7 42.1 41 A LEU N 315 209.6 100.3 44.0 41 A LEU CA 315 209.8 99.0 44.5 39 A LEU CB 315 210.6 99.0 45.8 40 A LEU CG 315 211.9 99.9 45.8 41 A LEU CD1 315 212.3 100.0 47.3 40 A LEU CD2 315 213.0 99.3 44.9 40 A LEU C 315 208.5 98.2 44.7 40 A LEU O 315 208.4 97.1 44.4 41 A VAL N 316 207.5 98.9 45.3 40 A VAL CA 316 206.2 98.3 45.5 41 A VAL CB 316 205.3 99.3 46.3 41 A VAL CG1 316 203.9 98.6 46.5 40 A VAL CG2 316 205.8 99.7 47.6 41 A VAL C 316 205.6 98.0 44.1 43 A VAL O 316 204.9 97.0 44.0 44 A ASP N 317 206.0 98.8 43.1 44 A ASP CA 317 205.5 98.6 41.8 45 A ASP CB 317 205.8 99.8 40.8 46 A ASP CG 317 204.9 100.9 41.1 48 A ASP OD1 317 203.7 100.7 41.4 48 A ASP OD2 317 205.4 102.1 41.1 48 A ASP C 317 206.1 97.3 41.2 44 A ASP O 317 205.5 96.6 40.5 44 A ILE N 318 207.4 97.1 41.4 44 A ILE CA 318 208.1 95.9 41.0 44 A ILE CB 318 209.6 96.0 41.3 43 A ILE CG2 318 210.3 94.7 40.8 44 A ILE CG1 318 210.2 97.2 40.5 43 A ILE CD1 318 211.7 97.3 40.7 42 A ILE C 318 207.5 94.7 41.6 45 A ILE O 318 207.1 93.7 41.0 45 A TYR N 319 207.4 94.8 43.0 47 A TYR CA 319 206.9 93.7 43.7 50 A TYR CB 319 206.9 94.0 45.2 50 A TYR CG 319 208.3 94.1 45.8 50 A TYR CD1 319 208.6 94.8 47.0 50 A TYR CE1 319 209.9 95.0 47.4 50 A TYR CD2 319 209.4 93.6 45.1 50 A TYR CE2 319 210.7 93.7 45.6 50 A TYR CZ 319 210.9 94.4 46.7 50 A TYR OH 319 212.2 94.5 47.2 51 A TYR C 319 205.5 93.3 43.3 52 A TYR O 319 205.2 92.1 43.1 53 A GLU N 320 204.7 94.3 43.0 54 A GLU CA 320 203.3 94.0 42.5 56 A GLU CB 320 202.6 95.4 42.2 58 A GLU CG 320 202.2 96.2 43.4 61 A GLU CD 320 201.8 97.6 43.0 63 A GLU OE1 320 200.7 98.1 43.4 65 A GLU OE2 320 202.6 98.4 42.4 64 A GLU C 320 203.3 93.2 41.3 56 A GLU O 320 202.7 92.2 41.2 56 A ASP N 321 204.2 93.6 40.4 56 A ASP CA 321 204.3 92.8 39.1 56 A ASP CB 321 205.0 93.7 38.0 55 A ASP CG 321 204.9 93.0 36.7 55 A ASP OD1 321 203.8 92.7 36.3 55 A ASP OD2 321 205.9 92.8 36.0 54 A ASP C 321 205.0 91.5 39.2 58 A ASP O 321 204.7 90.6 38.4 58 A MET N 322 205.9 91.3 40.2 60 A MET CA 322 206.5 90.0 40.3 61 A MET CB 322 207.7 90.1 41.3 61 A MET CG 322 208.9 90.9 40.7 61 A MET SD 322 210.5 90.5 41.5 61 A MET CE 322 210.3 91.5 42.9 59 A MET C 322 205.5 89.0 40.8 63 A MET O 322 205.5 87.9 40.3 64 A LEU N 323 204.7 89.4 41.8 66 A LEU CA 323 203.7 88.5 42.3 69 A LEU CB 323 202.9 89.1 43.4 68 A LEU CG 323 203.3 88.8 44.9 68 A LEU CD1 323 204.8 88.9 45.1 67 A LEU CD2 323 202.6 89.8 45.8 68 A LEU C 323 202.8 88.1 41.2 72 A LEU O 323 202.5 86.9 40.9 73 A GLU N 324 202.3 89.1 40.4 75 A GLU CA 324 201.4 88.9 39.3 78 A GLU CB 324 201.2 90.2 38.5 79 A GLU CG 324 200.3 91.3 39.3 81 A GLU CD 324 200.5 92.7 38.6 83 A GLU OE1 324 200.6 92.8 37.4 83 A GLU OE2 324 200.4 93.7 39.4 83 A GLU C 324 202.0 87.9 38.3 79 A GLU O 324 201.3 87.1 37.8 79 A ASN N 325 203.3 88.0 38.1 80 A ASN CA 325 204.0 87.1 37.1 81 A ASN CB 325 205.0 87.9 36.3 81 A ASN CG 325 204.3 89.0 35.4 81 A ASN OD1 325 204.6 90.1 35.3 81 A ASN ND2 325 203.2 88.5 34.8 81 A ASN C 325 204.7 85.9 37.8 81 A ASN O 325 205.8 85.5 37.4 81 A GLN N 326 204.0 85.4 38.8 84 A GLN CA 326 204.4 84.3 39.6 86 A GLN CB 326 203.9 83.0 38.9 87 A GLN CG 326 202.5 83.0 38.3 87 A GLN CD 326 202.4 83.3 36.8 88 A GLN OE1 326 202.9 82.5 36.0 88 A GLN NE2 326 201.7 84.4 36.5 88 A GLN C 326 205.9 84.2 39.9 87 A GLN O 326 206.6 83.2 39.5 87 A CYS N 327 206.4 85.1 40.6 89 A CYS CA 327 207.8 55.1 41.0 90 A CYS CB 327 208.3 86.5 41.5 89 A CYS SG 327 207.7 87.0 43.1 88 A CYS C 327 208.0 84.2 42.2 92 A CYS O 327 207.0 83.8 42.8 92 A ASP N 328 209.2 83.7 42.4 93 A ASP CA 328 209.5 82.8 43.5 94 A ASP CB 328 210.7 81.9 43.2 95 A ASP CG 328 210.3 80.4 43.4 96 A ASP OD1 328 210.3 79.7 42.4 97 A ASP OD2 328 210.0 80.0 44.6 96 A ASP C 328 209.8 83.7 44.7 94 A ASP O 328 210.3 84.9 44.6 95 A ASN N 329 209.5 83.3 45.9 94 A ASN CA 329 209.6 84.0 47.2 94 A ASN CB 329 210.7 85.0 47.2 94 A ASN CG 329 212.1 84.4 47.2 95 A ASN OD1 329 212.5 83.7 46.2 95 A ASN ND2 329 212.8 84.5 48.3 95 A ASN C 329 208.3 84.7 47.5 94 A ASN O 329 208.3 85.6 48.3 93 A LYS N 330 207.2 84.3 46.8 93 A LYS CA 330 205.9 85.0 47.0 93 A LYS CB 330 204.8 84.0 46.5 93 A LYS CG 330 203.8 84.7 45.6 95 A LYS CD 330 202.8 83.7 45.0 95 A LYS CE 330 201.8 84.4 44.0 95 A LYS NZ 330 202.5 84.8 42.8 94 A LYS C 330 205.6 85.4 48.4 92 A LYS O 330 205.3 86.6 48.6 92 A GLU N 331 205.9 84.6 49.4 92 A GLU CA 331 205.7 84.9 50.8 91 A GLU CB 331 206.0 83.7 51.7 93 A GLU CG 331 205.1 82.4 51.5 94 A GLU CD 331 203.8 82.5 52.1 95 A GLU OE1 331 203.0 81.5 51.9 95 A GLU OE2 331 203.4 83.5 52.7 96 A GLU C 331 206.6 86.1 51.2 89 A GLU O 331 206.1 87.0 51.9 89 A ASP N 332 207.9 85.9 50.9 87 A ASP CA 332 208.9 86.9 51.2 85 A ASP CB 332 210.3 86.2 50.7 87 A ASP CG 332 211.4 87.2 50.7 88 A ASP OD1 332 212.2 87.2 49.7 88 A ASP OD2 332 211.6 88.0 51.7 89 A ASP C 332 208.7 88.2 50.5 83 A ASP O 332 208.5 89.3 51.1 83 A ILE N 333 208.7 88.2 49.1 81 A ILE CA 333 208.6 89.4 48.4 77 A ILE CB 333 208.7 89.1 46.8 77 A ILE CG2 333 208.0 90.2 46.0 77 A ILE CG1 333 210.2 89.0 46.5 76 A ILE CD1 333 210.5 88.8 45.1 76 A ILE C 333 207.3 90.2 48.7 76 A ILE O 333 207.2 91.4 48.8 76 A LEU N 334 206.2 89.4 49.0 74 A LEU CA 334 204.9 90.0 49.4 73 A LEU CB 334 203.9 89.0 49.7 73 A LEU CG 334 202.5 89.4 50.3 73 A LEU CD1 334 201.9 90.5 49.4 73 A LEU CD2 334 201.6 88.2 50.3 73 A LEU C 334 205.1 90.9 50.7 73 A LEU O 334 204.8 92.0 50.7 74 A ASN N 335 205.8 90.3 51.7 73 A ASN CA 335 206.0 91.0 53.0 73 A ASN CB 335 206.8 90.2 53.9 74 A ASN CG 335 206.1 89.0 54.5 74 A ASN OD1 335 205.0 89.2 55.1 75 A ASN ND2 335 206.6 87.8 54.4 74 A ASN C 335 206.6 92.4 52.8 71 A ASN O 335 206.2 93.4 53.4 71 A LYS N 336 207.7 92.4 51.9 70 A LYS CA 336 208.3 93.6 51.6 69 A LYS CB 336 209.5 93.4 50.6 70 A LYS CG 336 210.9 93.4 51.3 71 A LYS CD 336 211.9 92.6 50.4 72 A LYS CE 336 211.5 91.2 50.1 72 A LYS NZ 336 212.4 90.5 49.2 73 A LYS C 336 207.3 94.6 51.0 68 A LYS O 336 207.2 95.7 51.6 67 A ALA N 337 206.7 94.2 50.0 66 A ALA CA 337 205.7 95.1 49.3 64 A ALA CB 337 204.9 94.2 48.3 63 A ALA C 337 204.7 95.7 50.4 63 A ALA O 337 204.5 96.9 50.4 63 A LEU N 338 204.2 94.8 51.2 62 A LEU CA 338 203.2 95.2 52.3 61 A LEU CB 338 202.6 94.0 52.9 61 A LEU CG 338 201.7 93.1 52.1 61 A LEU CD1 338 201.6 91.7 52.7 61 A LEU CD2 338 200.3 93.7 51.9 61 A LEU C 338 203.9 96.1 53.3 60 A LEU O 338 203.2 97.0 53.9 59 A GLU N 339 205.2 95.9 53.6 60 A GLU CA 339 205.9 96.7 54.6 61 A GLU CB 339 207.3 96.1 54.8 64 A GLU CG 339 208.2 96.9 55.8 67 A GLU CD 339 209.7 96.5 55.6 69 A GLU OE1 339 210.0 95.3 55.7 70 A GLU OE2 339 210.5 97.4 55.5 70 A GLU C 339 206.0 98.1 54.1 59 A GLU O 339 205.7 99.1 54.8 58 A LEU N 340 206.5 98.2 52.8 57 A LEU CA 340 206.7 99.5 52.2 55 A LEU CB 340 207.3 99.3 50.8 54 A LEU CG 340 208.6 98.4 50.7 54 A LEU CD1 340 209.3 98.7 49.3 53 A LEU CD2 340 209.5 98.7 51.8 54 A LEU C 340 205.4 100.2 52.1 55 A LEU O 340 205.3 101.4 52.5 55 A CYS N 341 204.3 99.5 51.8 55 A CYS CA 341 203.0 100.1 51.7 55 A CYS CB 341 201.9 99.1 51.3 54 A CYS SG 341 202.0 95.5 49.6 54 A CYS C 341 202.6 100.8 53.1 55 A CYS O 341 201.9 101.8 53.1 55 A GLU N 342 203.1 100.2 54.1 55 A GLU CA 342 202.8 100.7 55.5 55 A GLU CB 342 202.9 99.6 56.5 56 A GLU CG 342 202.1 100.0 57.8 57 A GLU CD 342 200.7 100.5 57.5 58 A GLU OE1 342 200.3 101.6 57.9 58 A GLU OE2 342 199.9 99.7 56.8 58 A GLU C 342 203.8 101.8 55.8 55 A GLU O 342 203.4 102.8 56.4 54 A ILE N 343 205.1 101.7 55.5 54 A ILE CA 343 206.1 102.7 55.7 54 A ILE CB 343 207.4 102.4 55.1 53 A ILE CG2 343 208.4 103.6 55.2 53 A ILE CG1 343 208.1 101.2 55.8 53 A ILE CD1 343 209.5 100.9 55.3 53 A ILE C 343 205.5 104.0 55.1 54 A ILE O 343 205.5 105.1 55.7 55 A LEU N 344 205.1 103.9 53.8 53 A LEU CA 344 204.6 105.0 53.1 52 A LEU CB 344 204.2 104.5 51.6 51 A LEU CG 344 205.4 104.1 50.7 50 A LEU CD1 344 204.9 103.5 49.4 49 A LEU CD2 344 206.3 105.3 50.4 50 A LEU C 344 203.3 105.5 53.7 53 A LEU O 344 203.2 106.6 54.2 54 A ALA N 345 202.3 104.6 53.9 54 A ALA CA 345 201.1 105.0 54.5 55 A ALA CB 345 200.2 103.8 54.7 55 A ALA C 345 201.2 105.7 55.9 56 A ALA O 345 200.4 106.7 56.1 57 A LYS N 346 202.0 105.2 56.8 58 A LYS CA 346 202.2 105.8 58.1 60 A LYS CB 346 202.6 104.7 59.1 62 A LYS CG 346 201.5 103.9 59.7 64 A LYS CD 346 202.1 102.9 60.7 67 A LYS CE 346 201.1 101.8 61.2 68 A LYS NZ 346 201.7 100.8 62.1 69 A LYS C 346 203.3 106.9 58.2 60 A LYS O 346 203.1 107.8 59.0 60 A GLU N 347 204.3 106.7 57.4 60 A GLU CA 347 205.5 107.6 57.5 60 A GLU CB 347 206.7 106.8 58.0 62 A GLU CG 347 208.0 107.6 58.0 65 A GLU CD 347 209.2 106.7 58.4 67 A GLU OE1 347 210.0 107.3 59.2 69 A GLU OE2 347 209.3 105.6 57.9 68 A GLU C 347 205.9 108.4 56.3 58 A GLU O 347 205.8 109.6 56.3 57 A LYS N 348 206.4 107.7 55.2 56 A LYS CA 348 206.9 108.4 54.0 55 A LYS CB 348 207.7 107.4 53.2 57 A LYS CG 348 208.7 106.6 54.0 57 A LYS CD 348 209.8 107.5 54.5 58 A LYS CE 348 210.9 106.7 55.3 59 A LYS NZ 348 211.5 105.6 54.5 59 A LYS C 348 205.9 109.1 53.1 54 A LYS O 348 206.3 110.1 52.4 54 A ASP N 349 204.7 108.7 53.0 51 A ASP CA 349 203.8 109.3 52.0 49 A ASP CB 349 203.8 108.6 50.7 49 A ASP CG 349 203.4 109.5 49.5 50 A ASP OD1 349 203.2 110.8 49.7 50 A ASP OD2 349 203.4 109.0 48.4 51 A ASP C 349 202.3 109.3 52.6 48 A ASP O 349 201.4 108.9 51.9 48 A THR N 350 202.2 109.9 53.8 46 A THR CA 350 200.9 109.9 54.5 46 A THR CB 350 201.1 110.5 55.9 46 A THR OG1 350 201.4 111.9 55.8 47 A THR CG2 350 202.2 109.8 56.6 46 A THR C 350 199.7 110.6 53.8 45 A THR O 350 198.6 110.3 54.1 44 A ILE N 351 200.0 111.5 52.9 45 A ILE CA 351 199.0 112.3 52.2 43 A ILE CB 351 199.6 113.4 51.3 41 A ILE CG2 351 200.3 112.8 50.1 41 A ILE CG1 351 198.5 114.3 50.9 40 A ILE CD1 351 198.1 115.3 52.0 39 A ILE C 351 198.1 111.2 51.4 43 A ILE O 351 196.8 111.4 51.4 43 A ARG N 352 198.6 110.1 51.0 43 A ARG CA 352 197.8 109.1 50.3 45 A ARG CB 352 198.2 108.9 48.8 44 A ARG CG 352 199.7 109.0 48.5 44 A ARG CD 352 199.9 109.7 47.1 43 A ARG NE 352 201.1 110.4 47.1 44 A ARG CZ 352 201.3 111.8 47.1 44 A ARG NH1 352 200.2 112.6 47.0 44 A ARG NH2 352 202.5 112.3 47.2 44 A ARG C 352 197.9 107.8 51.1 46 A ARG O 352 198.1 106.7 50.5 46 A LYS N 353 197.6 107.9 52.4 47 A LYS CA 353 197.5 106.7 53.3 46 A LYS CB 353 197.3 107.2 54.7 45 A LYS CG 353 196.0 107.9 55.0 45 A LYS CD 353 196.0 108.7 56.3 45 A LYS CE 353 194.6 109.4 56.5 45 A LYS NZ 353 194.5 110.3 57.7 45 A LYS C 353 196.3 105.9 52.8 47 A LYS O 353 196.4 104.6 52.8 46 A GLU N 354 195.3 106.5 52.4 48 A GLU CA 354 194.1 105.8 51.9 49 A GLU CB 354 193.0 106.8 51.5 51 A GLU CG 354 192.2 107.4 52.7 54 A GLU CD 354 191.5 106.3 53.5 56 A GLU OE1 354 191.9 106.1 54.7 57 A GLU OE2 354 190.5 105.7 53.1 57 A GLU C 354 194.4 104.9 50.7 48 A GLU O 354 194.0 103.8 50.5 49 A TYR N 355 195.3 105.4 49.8 47 A TYR CA 355 195.7 104.7 48.6 46 A TYR CB 355 196.3 105.7 47.6 43 A TYR CG 355 197.0 104.9 46.4 39 A TYR CD1 355 196.3 104.4 45.4 38 A TYR CE1 355 196.9 103.7 44.3 37 A TYR CD2 355 198.4 104.8 46.4 38 A TYR CE2 355 199.0 104.1 45.4 37 A TYR CZ 355 198.3 103.5 44.4 37 A TYR OH 355 198.9 102.8 43.3 37 A TYR C 355 196.7 103.6 48.9 47 A TYR O 355 196.5 102.5 48.5 48 A TRP N 356 197.7 104.0 49.6 48 A TRP CA 356 198.8 103.0 50.0 50 A TRP CB 356 199.9 103.7 50.7 50 A TRP CG 356 200.8 104.4 49.7 50 A TRP CD2 356 201.5 103.8 48.6 50 A TRP CE2 356 202.1 104.8 47.9 50 A TRP CE3 356 201.6 102.5 48.2 50 A TRP CD1 356 201.0 105.8 49.6 50 A TRP NE1 356 201.8 106.0 48.5 50 A TRP CZ2 356 202.9 104.6 46.8 50 A TRP CZ3 356 202.4 102.2 47.0 50 A TRP CH2 356 203.0 103.3 46.4 50 A TRP C 356 198.3 101.8 50.8 51 A TRP O 356 198.8 100.7 50.7 51 A ARG N 357 197.3 102.0 51.7 52 A ARG CA 357 196.7 100.9 52.4 53 A ARG CB 357 196.0 101.4 53.6 55 A ARG CG 357 196.8 101.5 54.9 57 A ARG CD 357 196.8 102.9 55.5 58 A ARG NE 357 195.4 103.2 55.7 60 A ARG CZ 357 195.0 104.2 56.6 61 A ARG NH1 357 193.7 104.4 56.7 61 A ARG NH2 357 195.9 104.9 57.2 61 A ARG C 357 195.9 100.1 51.5 53 A ARG O 357 196.0 98.8 51.6 54 A TYR N 358 195.2 100.7 50.6 52 A TYR CA 358 194.4 100.0 49.6 51 A TYR CB 358 193.7 100.9 48.7 51 A TYR CG 358 193.2 100.3 47.4 51 A TYR CD1 358 192.0 99.6 47.3 50 A TYR CE1 358 191.6 99.0 46.1 50 A TYR CD2 358 194.1 100.3 46.3 50 A TYR CE2 358 193.7 99.7 45.1 49 A TYR CZ 358 192.5 99.0 45.0 50 A TYR OH 358 192.2 98.4 43.9 50 A TYR C 358 195.3 99.0 48.9 51 A TYR O 358 194.9 97.9 48.6 50 A ILE N 359 196.5 99.4 48.6 51 A ILE CA 359 197.5 98.6 47.9 51 A ILE CB 359 198.8 99.4 47.6 50 A ILE CG2 359 199.8 98.5 47.0 49 A ILE CG1 359 198.4 100.5 46.6 50 A ILE CD1 359 197.8 99.9 45.3 49 A ILE C 359 197.9 97.4 48.8 52 A ILE O 359 198.1 96.3 48.3 51 A GLY N 360 197.9 97.6 50.1 53 A GLY CA 360 198.3 96.6 51.1 54 A GLY C 360 197.1 95.6 51.0 55 A GLY O 360 197.4 94.4 50.7 55 A ARG N 361 195.9 96.1 51.2 57 A ARG CA 361 194.7 95.2 51.2 58 A ARG CB 361 193.5 96.0 51.4 59 A ARG CG 361 193.0 96.1 52.9 60 A ARG CD 361 192.8 97.5 53.4 61 A ARG NE 361 191.7 98.1 52.6 62 A ARG CZ 361 191.7 99.5 52.4 62 A ARG NH1 361 190.7 100.0 51.6 63 A ARG NH2 361 192.7 100.2 52.9 63 A ARG C 361 194.6 94.4 49.9 59 A ARG O 361 194.2 93.3 49.9 61 A SER N 362 194.9 95.1 48.8 60 A SER CA 362 194.8 94.4 47.5 60 A SER CB 362 195.0 95.4 46.3 59 A SER OG 362 193.8 96.1 46.1 59 A SER C 362 195.9 93.3 47.4 59 A SER O 362 195.6 92.2 47.1 59 A LEU N 363 197.1 93.7 47.8 60 A LEU CA 363 198.2 92.7 47.8 62 A LEU CB 363 199.5 93.4 48.3 62 A LEU CG 363 200.5 93.8 47.2 62 A LEU CD1 363 199.8 94.7 46.1 62 A LEU CD2 363 201.6 94.6 47.8 62 A LEU C 363 197.9 91.6 48.7 63 A LEU O 363 198.4 90.5 48.6 62 A GLN N 364 197.1 91.9 49.7 65 A GLN CA 364 196.6 90.9 50.7 67 A GLN CB 364 195.8 91.6 51.8 68 A GLN CG 364 195.9 91.0 53.1 69 A GLN CD 364 197.3 91.2 53.7 70 A GLN OE1 364 197.4 92.0 54.7 71 A GLN NE2 364 198.3 90.4 53.3 70 A GLN C 364 195.8 89.8 50.0 68 A GLN O 364 195.8 88.7 50.5 69 A SER N 365 195.0 90.2 49.0 69 A SER CA 365 194.2 89.1 48.3 70 A SER CB 365 192.8 89.6 48.2 70 A SER OG 365 192.6 90.7 47.4 71 A SER C 365 194.8 88.7 47.0 72 A SER O 365 194.0 88.4 46.1 72 A LYS N 366 196.1 88.6 46.8 74 A LYS CA 366 196.8 88.2 45.6 77 A LYS CB 366 196.3 88.9 44.4 78 A LYS CG 366 196.5 90.4 44.3 80 A LYS CD 366 195.3 91.2 44.6 81 A LYS CE 366 194.1 90.8 43.8 82 A LYS NZ 366 192.8 91.6 44.3 83 A LYS C 366 198.3 88.1 45.7 77 A LYS OT1 366 198.8 87.5 46.7 77 A LYS OT2 366 199.0 88.6 44.7 76 A LEU CB 523 194.6 121.6 61.6 44 B LEU CG 523 193.3 122.3 62.1 44 B LEU CD1 523 193.5 123.8 61.8 44 B LEU CD2 523 192.1 121.8 61.4 44 B LEU C 523 195.8 119.4 61.4 46 B LEU O 523 196.9 119.6 61.9 46 B LEU N 523 194.6 119.9 63.4 47 B LEU CA 523 194.5 120.1 62.0 45 B TYR N 524 195.5 118.4 60.5 47 B TYR CA 524 196.6 117.6 59.9 46 B TYR CB 524 196.0 116.7 58.9 45 B TYR CG 524 197.0 116.0 58.0 45 B TYR CD1 524 197.6 114.8 58.3 44 B TYR CE1 524 198.6 114.1 57.5 44 B TYR CD2 524 197.3 116.5 56.7 44 B TYR CE2 524 198.3 115.9 55.9 43 B TYR CZ 524 198.9 114.7 56.3 43 B TYR OH 524 199.7 114.1 55.4 41 B TYR C 524 197.7 118.4 59.3 47 B TYR O 524 198.9 118.1 59.5 47 B SER N 525 197.3 119.5 58.7 48 B SER CA 525 198.3 120.4 58.0 50 B SER CB 525 197.6 121.3 57.0 49 B SER OG 525 196.6 122.0 57.6 49 B SER C 525 199.1 121.2 59.1 52 B SER O 525 200.3 121.5 58.8 53 B LEU N 526 198.5 121.5 60.2 54 B LEU CA 526 199.1 122.3 61.2 56 B LEU CB 526 198.0 123.0 62.0 56 B LEU CG 526 198.2 124.6 62.1 56 B LEU CD1 526 199.1 125.0 60.9 57 B LEU CD2 526 196.8 125.2 61.9 56 B LEU C 526 200.0 121.4 62.1 57 B LEU O 526 200.6 121.9 63.1 57 B ARG N 527 200.0 120.1 61.8 58 B ARG CA 527 200.8 119.2 62.6 58 B ARG CB 527 200.4 117.8 62.1 59 B ARG CG 527 200.7 116.7 63.1 59 B ARG CD 527 199.9 115.4 62.8 60 B ARG NE 527 198.5 115.7 63.1 60 B ARG CZ 527 197.5 114.9 62.5 60 B ARG NH1 527 197.8 113.9 61.7 60 B ARG NH2 527 196.3 115.2 62.8 60 B ARG C 527 202.2 119.4 62.4 59 B ARG O 527 202.7 119.8 61.4 61 B PRO N 528 203.0 119.2 63.5 60 B PRO CD 528 202.6 119.0 64.9 61 B PRO CA 528 204.5 119.5 63.5 61 B PRO CB 528 204.9 119.1 65.0 61 B PRO CG 528 203.7 119.6 65.7 60 B PRO C 528 205.3 118.7 62.6 61 B PRO O 528 206.3 119.1 62.0 61 B GLU N 529 204.9 117.4 62.3 62 B GLU CA 529 205.7 116.6 61.4 63 B GLU CB 529 205.3 115.1 61.7 65 B GLU CG 529 203.8 114.8 61.9 67 B GLU CD 529 203.4 114.8 63.3 69 B GLU OE1 529 202.7 113.8 63.7 70 B GLU OE2 529 203.7 115.8 64.1 70 B GLU C 529 205.4 116.9 60.0 63 B GLU O 529 206.2 116.6 59.1 62 B HIS N 530 204.2 117.5 59.7 62 B HIS CA 530 203.8 117.9 58.4 61 B HIS CB 530 202.4 118.5 58.4 62 B HIS CG 530 201.9 119.0 57.1 62 B HIS CD2 530 201.2 118.4 56.1 62 B HIS ND1 530 202.1 120.3 56.6 62 B HIS CE1 530 201.5 120.4 55.5 62 B HIS NE2 530 201.0 119.3 55.1 62 B HIS C 530 204.8 118.8 57.7 60 B HIS O 530 204.8 118.9 56.5 60 B ALA N 531 205.6 119.5 58.5 60 B ALA CA 531 206.6 120.4 58.0 59 B ALA CB 531 207.3 121.2 59.1 60 B ALA C 531 207.7 119.6 57.2 58 B ALA O 531 208.4 120.2 56.3 58 B ARG N 532 207.8 118.3 57.4 57 B ARG CA 532 208.8 117.5 56.7 56 B ARG CB 532 209.0 116.2 57.5 59 B ARG CG 532 209.9 116.3 58.7 63 B ARG CD 532 209.1 116.1 60.0 65 B ARG NE 532 208.9 114.6 60.2 68 B ARG CZ 532 208.6 114.1 61.4 69 B ARG NH1 532 208.3 114.9 62.5 69 B ARG NH2 532 208.4 112.8 61.5 69 B ARG C 532 208.3 117.3 55.3 54 B ARG O 532 209.1 116.8 54.4 53 B GLU N 533 207.0 117.6 55.1 51 B GLU CA 533 206.4 117.4 53.8 50 B GLU CB 533 204.9 117.3 53.9 49 B GLU CG 533 204.4 116.0 54.6 47 B GLU CD 533 204.9 114.7 53.8 46 B GLU OE1 533 204.0 114.0 53.3 46 B GLU OE2 533 206.1 114.4 53.7 45 B GLU C 533 206.8 118.5 52.8 50 B GLU O 533 206.3 118.6 51.7 50 B ARG N 534 207.7 119.3 53.2 50 B ARG CA 534 208.2 120.4 52.4 49 B ARG CB 534 209.1 121.3 53.3 50 B ARG CG 534 208.9 122.8 53.0 52 B ARG CD 534 207.6 123.3 53.5 53 B ARG NE 534 207.3 124.7 53.1 55 B ARG CZ 534 208.2 125.7 53.4 56 B ARG NH1 534 209.3 125.4 54.0 58 B ARG NH2 534 207.8 126.9 53.2 57 B ARG C 534 209.0 119.9 51.2 48 B ARG O 534 209.6 118.9 51.3 48 B LEU N 535 208.9 120.7 50.2 47 B LEU CA 535 209.6 120.3 48.9 46 B LEU CB 535 209.4 121.4 47.9 44 B LEU CG 535 210.2 121.2 46.5 43 B LEU CD1 535 209.6 120.1 45.7 42 B LEU CD2 535 210.2 122.5 45.8 43 B LEU C 535 211.1 120.1 49.2 46 B LEU O 535 211.7 120.9 49.9 46 B GLN N 536 211.7 119.1 48.5 47 B GLN CA 536 213.1 118.8 48.5 49 B GLN CB 536 213.3 117.4 49.0 50 B GLN CG 536 212.7 117.1 50.3 52 B GLN CD 536 213.2 115.9 51.0 53 B GLN OE1 536 212.5 115.1 51.5 54 B GLN NE2 536 214.5 115.7 50.9 53 B GLN C 536 213.7 119.0 47.2 50 B GLN O 536 213.6 118.1 46.4 51 B ASP N 537 214.2 120.2 46.9 51 B ASP CA 537 214.8 120.5 45.6 52 B ASP CB 537 214.9 122.0 45.4 53 B ASP CG 537 216.2 122.6 45.9 53 B ASP OD1 537 216.8 122.0 46.9 54 B ASP OD2 537 216.7 123.6 45.4 53 B ASP C 537 216.1 119.8 45.1 52 B ASP O 537 216.6 120.1 44.1 52 B ASP N 538 216.6 118.9 46.0 53 B ASP CA 538 217.9 118.2 45.7 53 B ASP CB 538 217.7 117.3 44.5 53 B ASP CG 538 216.6 116.2 44.8 55 B ASP OD1 538 216.7 115.6 45.8 55 B ASP OD2 538 215.7 116.0 43.9 55 B ASP C 538 219.0 119.2 45.4 52 B ASP O 538 220.1 118.8 44.9 52 B SER N 539 218.8 120.4 45.7 51 B SER CA 539 219.8 121.5 45.5 52 B SER CB 539 221.1 121.1 46.2 53 B SER OG 539 220.9 121.0 47.6 54 B SER C 539 220.1 121.7 44.0 52 B SER O 539 221.2 122.1 43.6 53 B VAL N 540 219.1 121.4 43.2 50 B VAL CA 540 219.1 121.6 41.8 48 B VAL CB 540 219.1 120.3 41.0 47 B VAL CG1 540 219.1 120.6 39.5 47 B VAL CG2 540 220.2 119.4 41.4 47 B VAL C 540 217.9 122.4 41.5 48 B VAL O 540 216.8 121.9 41.4 48 B GLU N 541 218.0 123.8 41.4 47 B GLU CA 541 216.9 124.6 41.2 46 B GLU CB 541 217.1 126.0 41.7 49 B GLU CG 541 217.8 126.1 43.0 54 B GLU CD 541 218.0 127.6 43.4 56 B GLU OE1 541 218.3 128.4 42.5 58 B GLU OE2 541 217.7 127.9 44.6 58 B GLU C 541 216.5 124.7 39.7 44 B GLU O 541 217.4 124.8 38.9 44 B THR N 542 215.2 124.7 39.5 42 B THR CA 542 214.7 124.9 38.1 39 B THR CB 542 214.3 123.6 37.5 39 B THR OG1 542 213.4 122.9 38.3 39 B THR CG2 542 215.6 122.8 37.3 39 B THR C 542 213.5 125.8 38.3 38 B THR O 542 213.0 126.0 39.5 39 B VAL N 543 212.9 126.4 37.2 35 B VAL CA 543 211.8 127.2 37.3 32 B VAL CB 543 211.2 127.5 35.9 31 B VAL CG1 543 210.0 128.5 36.1 30 B VAL CG2 543 212.3 128.1 35.1 32 B VAL C 543 210.7 126.5 38.1 32 B VAL O 543 210.0 127.2 38.9 32 B THR N 544 210.5 125.2 38.0 32 B THR CA 544 209.5 124.4 38.6 31 B THR CB 544 209.5 122.9 38.1 32 B THR OG1 544 209.4 122.9 36.7 32 B THR CG2 544 208.3 122.2 38.7 32 B THR C 544 209.6 124.4 40.2 30 B THR O 544 208.7 124.6 40.8 30 B SER N 545 210.8 124.1 40.7 31 B SER CA 545 211.0 124.0 42.1 32 B SER CB 545 212.4 123.4 42.5 31 B SER OG 545 213.4 123.9 41.7 32 B SER C 545 210.9 125.4 42.7 32 B SER O 545 210.3 125.6 43.7 34 B ILE N 546 211.5 126.4 42.0 33 B ILE CA 546 211.5 127.8 42.4 32 B ILE CB 546 212.1 128.7 41.3 32 B ILE CG2 546 211.8 130.1 41.5 31 B ILE CG1 546 213.6 128.4 41.3 32 B ILE CD1 546 214.4 129.1 40.2 33 B ILE C 546 210.0 128.2 42.6 33 B ILE O 546 209.7 128.9 43.6 35 B GLU N 547 209.1 127.9 41.7 33 B GLU CA 547 207.7 128.3 41.8 32 B GLU CB 547 207.0 128.2 40.5 34 B GLU CG 547 207.6 129.2 39.4 35 B GLU CD 547 207.4 130.6 39.9 36 B GLU OE1 547 206.3 131.0 40.3 37 B GLU OE2 547 208.4 131.4 39.8 38 B GLU C 547 207.0 127.5 42.8 32 B GLU O 547 206.0 128.0 43.5 31 B GLN N 548 207.3 126.2 42.9 32 B GLN CA 548 206.6 125.3 43.9 33 B GLN CB 548 207.1 123.9 43.7 31 B GLN CG 548 206.4 122.8 44.7 31 B GLN CD 548 204.9 122.8 44.8 32 B GLN OE1 548 204.3 122.6 45.8 32 B GLN NE2 548 204.3 123.1 43.6 33 B GLN C 548 207.0 125.8 45.3 33 B GLN O 548 206.1 126.0 46.2 33 B ALA N 549 208.3 126.2 45.5 34 B ALA CA 549 208.8 126.8 46.7 35 B ALA CB 549 210.3 127.0 46.6 34 B ALA C 549 208.1 128.1 47.1 36 B ALA O 549 207.8 128.3 48.3 37 B LYS N 550 207.8 128.9 46.1 37 B LYS CA 550 207.1 130.2 46.4 39 B LYS CB 550 207.0 131.0 45.2 41 B LYS CG 550 208.3 131.5 44.6 43 B LYS CD 550 208.1 132.4 43.4 45 B LYS CE 550 209.4 132.8 42.7 46 B LYS NZ 550 209.2 133.7 41.5 47 B LYS C 550 205.8 129.9 47.0 40 B LYS O 550 205.3 130.5 47.9 41 B VAL N 551 205.1 128.9 46.3 40 B VAL CA 551 203.7 128.5 46.8 40 B VAL CB 551 203.1 127.5 45.8 40 B VAL CG1 551 201.8 127.0 46.4 40 B VAL CG2 551 202.8 128.2 44.5 40 B VAL C 551 203.7 128.0 48.2 41 B VAL O 551 203.0 128.5 49.0 41 B GLU N 552 204.6 127.0 48.4 41 B GLU CA 552 204.7 126.4 49.7 43 B GLU CB 552 205.7 125.3 49.8 41 B GLU CG 552 205.4 124.1 49.0 39 B GLU CD 552 206.4 123.0 49.1 38 B GLU OE1 552 207.5 123.3 49.7 37 B GLU OE2 552 206.1 121.9 48.7 38 B GLU C 552 204.9 127.4 50.8 45 B GLU O 552 204.2 127.4 51.8 46 B GLU N 553 205.8 128.4 50.6 48 B GLU CA 553 206.1 129.4 51.5 50 B GLU CB 553 207.1 130.4 50.9 53 B GLU CG 553 207.4 131.6 51.8 57 B GLU CD 553 208.8 131.6 52.3 60 B GLU OE1 553 209.1 130.6 53.1 61 B GLU OE2 553 209.6 132.5 52.0 61 B GLU C 553 204.8 130.2 51.9 49 B GLU O 553 204.6 130.4 53.1 49 B LYS N 554 204.1 130.6 51.0 49 B LYS CA 554 202.8 131.3 51.3 51 B LYS CB 554 202.1 131.8 50.0 53 B LYS CG 554 203.0 132.7 49.2 57 B LYS CD 554 202.2 133.2 47.9 61 B LYS CE 554 203.0 134.2 47.1 63 B LYS NZ 554 202.1 135.0 46.2 64 B LYS C 554 201.9 130.5 52.1 51 B LYS O 554 201.2 131.0 53.0 51 B ILE N 555 201.7 129.2 51.7 51 B ILE CA 555 200.8 128.3 52.4 50 B ILE CB 555 200.7 126.9 51.7 49 B ILE CG2 555 199.7 126.1 52.4 48 B ILE CG1 555 200.4 127.1 50.2 49 B ILE CD1 555 199.2 127.9 49.9 49 B ILE C 555 201.3 128.1 53.8 50 B ILE O 555 200.5 128.2 54.8 50 B GLN N 556 202.6 127.9 54.0 50 B GLN CA 556 203.2 127.8 55.3 51 B GLN CB 556 204.7 127.8 55.1 51 B GLN CG 556 205.5 127.7 56.4 53 B GLN CD 556 205.1 126.4 57.2 53 B GLN OE1 556 205.9 125.4 57.1 55 B GLN NE2 556 204.0 126.4 57.9 53 B GLN C 556 202.7 128.9 56.1 53 B GLN O 556 202.1 128.7 57.1 54 B GLU N 557 203.0 130.2 55.7 53 B GLU CA 557 202.6 131.3 56.4 54 B GLU CB 557 202.9 132.6 55.6 57 B GLU CG 557 204.4 132.7 55.2 60 B GLU CD 557 204.7 133.9 54.3 62 B GLU OE1 557 203.9 134.8 54.2 63 B GLU OE2 557 205.9 134.0 53.8 62 B GLU C 557 201.1 131.3 56.8 54 B GLU O 557 200.8 131.8 57.9 55 B VAL N 558 200.3 130.8 56.0 54 B VAL CA 558 198.8 130.7 56.3 53 B VAL CB 558 198.0 130.2 55.1 53 B VAL CG1 558 196.6 129.9 55.5 53 B VAL CG2 558 198.0 131.2 53.9 53 B VAL C 558 198.6 129.7 57.4 52 B VAL O 558 197.9 130.0 58.4 52 B PHE N 559 199.2 128.6 57.4 52 B PHE CA 559 199.1 127.6 58.4 52 B PHE CB 559 199.9 126.3 58.0 50 B PHE CG 559 199.3 125.6 56.8 49 B PHE CD1 559 200.0 124.7 56.1 49 B PHE CD2 559 197.9 125.8 56.5 48 B PHE CE1 559 199.4 123.9 55.0 47 B P HE CE2 559 197.3 125.0 55.5 47 B PHE CZ 559 198.1 124.1 54.7 48 B PHE C 559 199.5 128.1 59.8 53 B PHE O 559 198.8 128.0 60.7 53 B SER N 560 200.7 128.8 59.8 54 B SER CA 560 201.2 129.3 61.0 56 B SER CB 560 202.7 129.6 60.9 55 B SER OG 560 203.4 128.4 60.4 55 B SER C 560 200.5 130.6 61.4 58 B SER O 560 200.8 131.1 62.5 57 B SER N 561 199.6 131.2 60.6 61 B SER CA 561 199.0 132.4 61.0 64 B SER CB 561 198.0 132.9 59.9 64 B SER OG 561 196.9 132.0 59.8 64 B SER C 561 198.2 132.1 62.3 66 B SER O 561 198.2 132.9 63.2 66 B TYR N 562 197.7 130.9 62.4 70 B TYR CA 562 196.9 130.4 63.5 73 B TYR CB 562 196.3 129.0 63.2 73 B TYR CG 562 195.2 129.0 62.2 73 B TYR CD1 562 195.4 128.5 60.9 73 B TYR CE1 562 194.4 128.5 59.9 74 B TYR CD2 562 194.0 129.6 62.5 73 B TYR CE2 562 193.0 129.7 61.5 74 B TYR CZ 562 193.2 129.1 60.2 74 B TYR OH 562 192.2 129.2 59.3 74 B TYR C 562 197.8 130.3 64.8 75 B TYR O 562 197.5 131.0 65.8 75 B LYS N 563 198.8 129.5 64.7 77 B LYS CA 563 199.8 129.3 65.7 79 B LYS CB 563 200.7 128.1 65.2 81 B LYS CG 563 201.1 127.1 66.2 82 B LYS CD 563 201.5 125.8 65.6 83 B LYS CE 563 202.8 125.9 64.7 84 B LYS NZ 563 203.8 124.8 65.0 84 B LYS C 563 200.7 130.5 65.9 80 B LYS O 563 201.9 130.4 66.1 79 B PHE N 564 200.0 131.7 66.0 82 B PHE CA 564 200.7 133.0 66.2 85 B PHE CB 564 200.4 133.8 65.0 87 B PHE CG 564 201.1 135.2 65.0 90 B PHE CD1 564 202.4 135.4 64.6 91 B PHE CD2 564 200.4 136.3 65.5 91 B PHE CE1 564 203.0 136.7 64.6 92 B PHE CE2 564 200.9 137.6 65.6 92 B PHE CZ 564 202.3 137.8 65.2 93 B PHE C 564 200.3 133.7 67.5 85 B PHE O 564 199.4 134.6 67.4 85 B ASN N 565 200.9 133.3 68.6 84 B ASN CA 565 200.6 133.9 69.9 82 B ASN CB 565 201.4 135.2 70.1 84 B ASN CG 565 202.7 135.0 70.8 86 B ASN OD1 565 203.0 133.9 71.2 87 B ASN ND2 565 203.5 136.1 70.9 87 B ASN C 565 199.2 134.4 70.0 81 B ASN O 565 198.9 135.4 70.6 80 B HIS N 566 198.3 133.7 69.4 79 B HIS CA 566 196.9 134.2 69.4 78 B HIS CB 566 196.7 134.8 68.0 81 B HIS CG 566 196.4 136.3 68.0 82 B HIS CD2 566 195.3 137.0 68.2 83 B HIS ND1 566 197.5 137.2 67.9 83 B HIS CE1 566 197.0 138.5 67.9 83 B HIS NE2 566 195.6 138.4 68.1 83 B HIS C 566 195.8 133.4 69.8 76 B HIS O 566 195.4 133.3 70.9 75 B LEU N 567 195.1 132.9 68.7 75 B LEU CA 567 193.9 132.2 68.9 74 B LEU CB 567 192.8 132.7 68.0 74 B LEU CG 567 192.6 134.2 67.8 74 B LEU CD1 567 192.9 135.0 69.1 73 B LEU CD2 567 193.5 134.7 66.6 73 B LEU C 567 194.0 130.7 68.7 74 B LEU O 567 195.2 130.2 68.5 75 B VAL N 568 192.9 130.0 68.6 74 B VAL CA 568 192.8 128.6 68.4 73 B VAL CB 568 191.8 127.9 69.4 73 B VAL CG1 568 191.9 126.4 69.4 73 B VAL CG2 568 192.1 128.5 70.8 72 B VAL C 568 192.2 128.5 67.0 72 B VAL O 568 191.2 129.1 66.7 73 B PRO N 569 192.8 127.7 66.1 71 B PRO CD 569 194.0 126.9 66.2 71 B PRO CA 569 192.2 127.6 64.7 71 B PRO CB 569 193.1 126.6 64.0 71 B PRO CG 569 193.8 125.9 65.1 71 B PRO C 569 190.7 127.2 64.7 70 B PRO O 569 190.3 126.2 65.2 70 B ARG N 570 189.9 128.1 64.1 70 B ARG CA 570 188.5 127.9 63.9 70 B ARG CB 570 187.8 129.2 64.4 73 B ARG CG 570 187.7 129.3 65.9 77 B ARG CD 570 186.3 128.8 66.4 80 B ARG NE 570 186.3 127.4 66.4 82 B ARG CZ 570 185.7 126.7 67.4 84 B ARG NH1 570 185.1 127.3 68.4 85 B ARG NH2 570 185.8 125.3 67.4 85 B ARG C 570 188.3 127.7 62.4 68 B ARG O 570 188.3 128.7 61.7 68 B LEU N 571 188.2 126.5 62.0 63 B LEU CA 571 188.0 126.3 60.6 59 B LEU CB 571 188.4 124.9 60.1 59 B LEU CG 571 189.7 124.8 59.3 58 B LEU CD1 571 190.9 125.3 60.1 57 B LEU CD2 571 189.9 123.4 58.7 57 B LEU C 571 186.5 126.6 60.3 57 B LEU O 571 185.6 125.9 60.9 57 B VAL N 572 186.2 127.6 59.5 55 B VAL CA 572 184.8 128.0 59.3 53 B VAL CB 572 184.4 129.2 60.2 53 B VAL CG1 572 183.0 129.6 59.9 53 B VAL CG2 572 184.7 128.9 61.6 54 B VAL C 572 184.6 128.4 57.8 53 B VAL O 572 185.4 129.2 57.2 53 B LEU N 573 183.5 128.0 57.2 51 B LEU CA 573 183.2 128.3 55.9 49 B LEU CB 573 182.4 127.2 55.2 48 B LEU CG 573 181.9 127.5 53.8 48 B LEU CD1 573 183.1 127.2 52.8 47 B LEU CD2 573 180.7 126.6 53.5 47 B LEU C 573 182.3 129.6 55.9 48 B LEU O 573 181.1 129.6 56.4 47 B GLN N 574 182.8 130.7 55.5 48 B GLN CA 574 182.1 132.0 55.5 48 B GLN CB 574 183.0 133.1 55.0 49 B GLN CG 574 184.4 133.1 55.7 51 B GLN CD 574 184.3 133.2 57.2 52 B GLN OE1 574 185.2 132.8 57.9 54 B GLN NE2 574 183.2 133.7 57.8 52 B GLN C 574 180.9 132.0 54.6 48 B GLN O 574 180.8 132.7 53.5 48 B ARG N 575 179.9 131.2 55.0 48 B ARG CA 575 178.6 131.0 54.2 48 B ARG CB 575 177.7 130.2 55.0 49 B ARG CG 575 178.1 128.7 55.2 50 B ARG CD 575 177.2 128.1 56.2 51 B ARG NE 575 177.2 126.6 56.1 51 B ARG CZ 575 176.6 125.9 55.1 51 B ARG NH1 575 175.8 126.5 54.3 50 B ARG NH2 575 176.7 124.6 55.1 51 B ARG C 575 177.9 132.3 53.8 49 B ARG O 575 177.5 132.5 52.7 48 B GLU N 576 177.7 133.2 54.8 49 B GLU CA 576 177.0 434.4 54.6 49 B GLU CB 576 176.7 135.2 55.9 52 B GLU CG 576 176.5 134.4 57.1 55 B GLU CD 576 175.3 133.4 57.0 57 B GLU OE1 576 174.3 133.8 56.3 58 B GLU OE2 576 175.4 132.3 57.5 58 B GLU C 576 177.7 135.3 53.6 47 B GLU O 576 177.1 135.8 52.6 46 B LYS N 577 179.0 135.3 53.7 46 B LYS CA 577 179.9 136.1 52.9 45 B LYS CB 577 181.3 136.0 53.4 46 B LYS CG 577 181.9 137.3 53.9 48 B LYS CD 577 180.9 138.1 54.8 50 B LYS CE 577 180.7 139.5 54.4 51 B LYS NZ 577 179.6 139.8 53.5 52 B LYS C 577 179.8 135.5 51.4 43 B LYS O 577 179.6 136.3 50.5 43 B HIS N 578 179.9 134.2 51.3 41 B HIS CA 578 179.8 133.6 50.0 38 B HIS CB 578 180.0 132.1 50.1 34 B HIS CG 578 181.3 131.7 50.7 31 B HIS CD2 578 181.8 130.6 51.3 30 B HIS ND1 578 182.4 132.6 50.7 30 B HIS CE1 578 183.5 131.9 51.3 29 B HIS NE2 578 183.1 130.7 51.6 29 B HIS C 578 178.4 133.8 49.4 39 B HIS O 578 178.2 134.0 48.2 39 B PHE N 579 177.4 133.7 50.3 40 B PHE CA 579 176.0 133.9 49.9 41 B PHE CB 579 175.1 133.6 51.0 41 B PHE CG 579 173.7 133.9 50.7 41 B PHE CD1 579 172.9 133.1 49.9 42 B PHE CD2 579 173.1 135.1 51.2 42 B PHE CE1 579 171.6 133.4 49.5 42 B PHE CE2 579 171.8 135.4 50.8 43 B PHE CZ 579 171.1 134.6 50.0 43 B PHE C 579 175.7 135.2 49.2 43 B PHE O 579 175.0 135.2 48.2 44 B HIS N 580 176.2 136.3 49.8 46 B HIS CA 580 175.9 137.6 49.3 47 B HIS CB 580 176.3 138.7 50.4 52 B HIS CG 580 175.8 138.4 51.7 55 B HIS CD2 580 174.5 138.2 52.2 57 B HIS ND1 580 176.6 138.3 52.8 57 B HIS CE1 580 175.9 138.0 53.9 58 B HIS NE2 580 174.6 137.9 53.5 58 B HIS C 580 176.6 137.9 48.0 46 B HIS O 580 176.2 138.6 47.2 45 B TYR N 581 177.8 137.3 48.0 44 B TYR CA 581 178.7 137.4 46.8 43 B TYR CB 581 180.0 136.7 47.1 42 B TYR CG 581 181.0 136.5 45.9 43 B TYR CD1 581 181.3 137.6 45.1 43 B TYR CE1 581 182.1 137.5 44.0 44 B TYR CD2 581 181.6 135.3 45.7 43 B TYR CE2 581 182.5 135.2 44.6 43 B TYR CZ 581 182.7 136.3 43.8 43 B TYR OH 581 183.6 136.1 42.7 43 B TYR C 581 178.0 136.7 45.6 42 B TYR O 581 177.8 137.4 44.5 41 B LEU N 582 177.6 135.5 45.8 41 B LEU CA 582 176.9 134.7 44.8 40 B LEU CB 582 176.7 133.3 45.4 38 B LEU CG 582 177.9 132.5 45.6 36 B LEU CD1 582 177.8 131.4 46.6 35 B LEU CD2 582 178.4 131.8 44.3 36 B LEU C 582 175.5 135.3 44.5 42 B LEU O 582 175.2 135.4 43.3 42 B LYS N 583 174.9 135.8 45.5 45 B LYS CA 583 173.6 136.4 45.4 47 B LYS CB 583 173.1 136.8 46.8 50 B LYS CG 583 171.8 137.6 47.0 53 B LYS CD 583 171.6 138.0 48.5 55 B LYS CE 583 170.6 139.2 48.6 56 B LYS NZ 583 169.2 138.9 48.4 56 B LYS C 583 173.6 137.7 44.5 47 B LYS O 583 172.7 137.8 43.6 47 B ARG N 584 174.6 138.6 44.6 48 B ARG CA 584 174.6 139.7 43.7 49 B ARG CB 584 175.3 140.9 44.2 53 B ARG CG 584 174.5 142.2 44.0 58 B ARG CD 584 175.2 143.5 44.0 62 B ARG NE 584 175.9 143.8 42.8 66 B ARG CZ 584 177.1 144.5 42.7 68 B ARG NH1 584 177.7 144.9 43.8 69 B ARG NH2 584 177.7 144.7 41.5 68 B ARG C 584 175.2 139.4 42.3 47 B ARG O 584 174.8 140.0 41.3 45 B GLY N 585 176.1 138.4 42.3 46 B GLY CA 585 176.7 138.0 41.0 44 B GLY C 585 175.7 137.3 40.1 42 B GLY O 585 175.8 137.3 38.9 40 B LEU N 586 174.6 136.7 40.7 41 B LEU CA 586 173.6 136.0 39.9 40 B LEU CB 586 172.7 135.2 40.8 40 B LEU CG 586 171.6 134.3 40.1 41 B LEU CD1 586 172.3 133.4 39.1 40 B LEU CD2 586 170.8 133.5 41.1 40 B LEU C 586 172.8 137.1 39.2 40 B LEU O 586 172.2 136.8 38.2 40 B ARG N 587 172.8 138.3 39.7 41 B ARG CA 587 172.1 139.4 39.0 41 B ARG CB 587 171.3 140.2 40.1 43 B ARG CG 587 169.8 140.1 40.0 46 B ARG CD 587 169.4 138.6 40.2 48 B ARG NE 587 168.0 138.5 40.6 51 B ARG CZ 587 166.9 138.5 39.7 52 B ARG NH1 587 167.2 138.6 38.4 52 B ARG NH2 587 165.7 138.4 40.2 53 B ARG C 587 172.9 140.3 38.2 40 B ARG O 587 172.5 140.6 37.1 39 B GLN N 588 174.1 140.7 38.7 39 B GLN CA 588 174.9 141.6 37.9 39 B GLN CB 588 174.5 143.1 38.0 41 B GLN CG 588 174.8 143.7 39.3 46 B GLN CD 588 174.4 145.2 39.3 48 B GLN OE1 588 173.7 145.7 38.4 49 B GLN NE2 588 174.8 145.9 40.4 50 B GLN C 588 176.4 141.5 38.2 37 B GLN O 588 176.8 141.2 39.4 36 B LEU N 589 177.2 141.7 37.2 34 B LEU CA 589 178.7 141.7 37.4 33 B LEU CB 589 179.2 140.4 36.8 31 B LEU CG 589 178.5 139.1 37.1 29 B LEU CD1 589 178.5 138.2 35.9 30 B LEU CD2 589 179.3 138.4 38.2 28 B LEU C 589 179.3 142.9 36.8 33 B LEU O 589 178.7 143.5 35.9 31 B THR N 590 180.5 143.3 37.3 33 B THR CA 590 181.2 144.4 36.7 34 B THR CB 590 182.3 144.9 37.7 35 B THR OG1 590 183.4 143.9 37.7 36 B THR CG2 590 181.8 145.0 39.1 36 B THR C 590 181.8 144.1 35.4 35 B THR O 590 181.8 143.0 35.0 36 B ASP N 591 182.3 145.1 34.7 33 B ASP CA 591 182.8 144.9 33.4 33 B ASP CB 591 183.1 146.2 32.6 33 B ASP CG 591 184.0 147.1 33.3 35 B ASP OD1 591 184.4 148.2 32.7 36 B ASP OD2 591 184.5 146.8 34.5 35 B ASP C 591 184.1 144.1 33.4 32 B ASP O 591 184.7 143.8 32.3 34 B ALA N 592 184.5 143.7 34.6 30 B ALA CA 592 185.7 142.8 34.7 28 B ALA CB 592 186.1 142.7 36.2 27 B ALA C 592 185.4 141.5 34.2 28 B ALA O 592 186.2 140.6 34.0 28 B TYR N 593 184.1 141.2 34.0 28 B TYR CA 593 183.5 140.0 33.5 28 B TYR CB 593 182.3 139.6 34.2 26 B TYR CG 593 182.6 138.9 35.5 26 B TYR CD1 593 182.9 139.6 36.7 26 B TYR CE1 593 183.4 138.9 37.8 26 B TYR CD2 593 182.8 137.5 35.4 26 B TYR CE2 593 183.3 136.8 36.6 26 B TYR CZ 593 183.6 137.5 37.7 26 B TYR OH 593 184.1 136.9 38.8 27 B TYR C 593 183.3 140.0 32.0 28 B TYR O 593 182.6 139.1 31.5 29 B GLU N 594 183.8 141.1 31.3 28 B GLU CA 594 183.6 141.2 29.9 28 B GLU CB 594 184.2 142.5 29.4 29 B GLU CG 594 183.4 143.7 29.8 31 B GLU CD 594 184.0 145.0 29.3 33 B GLU OE1 594 183.3 146.0 29.1 34 B GLU OE2 594 185.2 145.0 29.1 34 B GLU C 594 184.2 140.0 29.2 26 B GLU O 594 183.7 139.5 28.2 27 B CYS N 595 185.3 139.5 29.8 26 B CYS CA 595 186.0 138.3 29.2 25 B CYS CB 595 187.4 138.1 30.0 24 B CYS SG 595 187.3 137.7 31.7 23 B CYS C 595 185.2 137.0 29.4 24 B CYS O 595 185.6 135.9 28.8 23 B LEU N 596 184.1 137.0 30.1 23 B LEU CA 596 183.2 135.9 30.3 22 B LEU CB 596 183.1 135.6 31.8 22 B LEU CG 596 184.2 134.8 32.4 22 B LEU CD1 596 183.9 134.4 33.8 22 B LEU CD2 596 184.6 133.5 31.7 22 B LEU C 596 181.9 136.2 29.7 22 B LEU O 596 180.9 135.5 30.0 22 B ASP N 597 181.9 137.1 28.7 24 B ASP CA 597 180.7 137.5 28.0 24 B ASP CB 597 180.9 138.7 27.1 24 B ASP CG 597 179.6 139.2 26.5 24 B ASP OD1 597 178.6 139.2 27.3 25 B ASP OD2 597 179.6 139.7 25.4 25 B ASP C 597 180.2 136.3 27.1 26 B ASP O 597 179.0 136.4 26.6 27 B ALA N 598 181.0 135.3 26.8 26 B ALA CA 598 180.6 134.1 26.0 26 B ALA CB 598 181.6 133.9 24.9 25 B ALA C 598 180.5 132.9 26.9 27 B ALA O 598 180.6 131.8 26.4 27 B SER N 599 180.4 133.1 28.2 27 B SER CA 599 180.3 132.0 29.2 26 B SER CB 599 181.6 131.8 29.9 25 B SER OG 599 182.6 131.3 29.1 25 B SER C 599 179.2 132.3 30.1 26 B SER O 599 179.3 132.0 31.3 27 B ARG N 600 178.1 133.0 29.7 27 B ARG CA 600 177.1 133.3 30.6 28 B ARG CB 600 176.2 134.5 30.1 28 B ARG CG 600 177.1 135.7 30.1 28 B ARG CD 600 176.4 136.9 29.5 30 B ARG NE 600 175.4 137.4 30.5 30 B ARG CZ 600 174.3 138.1 30.1 30 B ARG NH1 600 174.1 138.4 28.8 30 B ARG NH2 600 173.4 138.5 31.0 32 B ARG C 600 176.3 132.1 31.2 28 B ARG O 600 176.0 132.1 32.4 31 B PRO N 601 176.1 131.1 30.5 26 B PRO CD 601 176.0 130.9 29.0 26 B PRO CA 601 175.4 130.0 31.1 25 B PRO CB 601 175.1 129.0 30.0 24 B PRO CG 601 174.9 129.9 28.8 24 B PRO C 601 176.3 129.4 32.2 25 B PRO O 601 175.8 128.8 33.1 27 B TRP N 602 177.6 129.6 32.0 26 B TRP CA 602 178.5 129.0 33.0 26 B TRP CB 602 180.0 129.2 32.5 25 B TRP CG 602 180.5 128.1 31.7 26 B TRP CD2 602 180.7 126.7 32.1 26 B TRP CE2 602 181.2 126.0 30.9 25 B TRP CE3 602 180.5 126.0 33.3 26 B TRP CD1 602 180.9 128.1 30.3 25 B TRP NE1 602 181.3 126.9 29.9 26 B TRP CZ2 602 181.5 124.6 31.0 26 B TRP CZ3 602 180.8 124.6 33.3 26 B TRP CH2 602 181.3 124.0 32.2 26 B TRP C 602 178.4 129.8 34.3 26 B TRP O 602 178.5 129.2 35.3 27 B LEU N 603 178.2 131.1 34.2 28 B LEU CA 603 178.0 131.9 35.4 28 B LEU CB 603 178.1 133.4 35.0 29 B LEU CG 603 179.5 133.9 34.7 30 B LEU CD1 603 179.5 135.2 34.0 29 B LEU CD2 603 180.4 133.9 36.0 28 B LEU C 603 176.8 131.5 36.1 28 B LEU O 603 176.8 131.5 37.3 29 B CYS N 604 175.7 131.2 35.4 28 B CYS CA 604 174.5 130.8 36.0 28 B CYS CB 604 173.4 130.6 34.9 29 B CYS SG 604 172.8 132.0 34.1 33 B CYS C 604 174.7 129.4 36.7 28 B CYS O 604 174.4 129.3 37.9 30 B TYR N 605 175.4 128.5 36.0 26 B TYR CA 605 175.6 127.2 36.6 24 B TYR CB 605 176.3 126.2 35.6 23 B TYR CG 605 176.9 125.0 36.3 22 B TYR CD1 605 176.1 124.1 37.0 22 B TYR CE1 605 176.7 123.0 37.7 21 B TYR CD2 605 178.3 124.8 36.3 22 B TYR CE2 605 178.8 123.8 37.0 23 B TYR CZ 605 178.0 122.9 37.7 22 B TYR OH 605 178.7 121.8 38.3 24 B TYR C 605 176.5 127.3 37.8 25 B TYR O 605 176.2 126.8 38.9 25 B TRP N 606 177.6 128.0 37.7 27 B TRP CA 606 178.6 128.2 38.8 28 B TRP CB 606 179.8 129.1 38.4 28 B TRP CG 606 180.7 128.5 37.3 28 B TRP CD2 606 181.5 129.2 36.4 28 B TRP CE2 606 182.3 128.3 35.6 28 B TRP CE3 606 181.7 130.6 36.1 29 B TRP CD1 606 181.1 127.2 37.1 27 B TRP NE1 606 182.0 127.1 36.1 26 B TRP CZ2 606 183.1 128.7 34.6 28 B TRP CZ3 606 182.5 131.0 35.1 28 B TRP CH2 606 183.3 130.1 34.3 28 B TRP C 606 177.9 128.8 40.0 29 B TRP O 606 178.1 128.2 41.1 31 B ILE N 607 177.2 129.8 39.8 31 B ILE CA 607 176.5 130.5 41.0 32 B ILE CB 607 176.0 131.9 40.6 31 B ILE CG2 607 175.1 132.5 41.7 30 B ILE CG1 607 177.2 132.8 40.2 30 B ILE CD1 607 176.9 134.0 39.4 30 B ILE C 607 175.3 129.6 41.5 32 B ILE O 607 175.4 129.2 42.7 32 B LEU N 608 174.4 129.3 40.7 32 B LEU CA 608 173.2 128.4 41.1 31 B LEU CB 608 172.4 128.1 39.9 30 B LEU CG 608 170.9 128.6 39.8 30 B LEU CD1 608 170.8 130.0 40.4 30 B LEU CD2 608 170.6 128.7 38.3 31 B LEU C 608 173.7 127.1 41.7 31 B LEU O 608 172.9 126.6 42.5 33 B HIS N 609 174.8 126.7 41.4 30 B HIS CA 609 175.3 125.4 42.0 30 B HIS CB 609 176.3 124.7 41.0 27 B HIS CG 609 176.8 123.4 41.6 25 B HIS CD2 609 178.1 123.0 41.8 24 B HIS ND1 609 176.1 122.4 42.1 24 B HIS CE1 609 176.9 121.5 42.6 24 B HIS NE2 609 178.1 121.8 42.5 24 B HIS C 609 176.0 125.7 43.3 31 B HIS O 609 175.8 124.9 44.2 31 B SER N 610 176.7 126.7 43.4 32 B SER CA 610 177.4 127.1 44.7 35 B SER CB 610 178.2 128.3 44.5 35 B SER OG 610 179.2 128.1 43.5 35 B SER C 610 176.3 127.3 45.8 35 B SER O 610 176.4 126.8 46.9 34 B LEU N 611 175.2 128.0 45.4 36 B LEU CA 611 174.1 128.2 46.3 37 B LEU CB 611 173.0 129.1 45.6 36 B LEU CG 611 173.5 130.5 45.2 35 B LEU CD1 611 172.3 131.2 44.5 35 B LEU CD2 611 173.9 131.2 46.4 35 B LEU C 611 173.5 126.9 46.7 39 B LEU O 611 173.3 126.6 47.9 40 B GLU N 612 173.3 126.0 45.7 40 B GLU CA 612 172.7 124.7 46.0 41 B GLU CB 612 172.7 123.9 44.6 43 B GLU CG 612 172.4 122.4 44.8 44 B GLU CD 612 173.2 121.5 43.8 45 B GLU OE1 612 174.0 120.7 44.4 45 B GLU OE2 612 173.1 121.7 42.6 45 B GLU C 612 173.6 123.9 47.0 41 B GLU O 612 173.1 123.3 47.9 42 B LEU N 613 174.9 124.1 46.8 41 B LEU CA 613 175.8 123.4 47.8 42 B LEU CB 613 177.2 123.5 47.3 40 B LEU CG 613 177.6 122.5 46.2 40 B LEU CD1 613 178.8 123.0 45.4 39 B LEU CD2 613 178.0 121.1 46.9 40 B LEU C 613 175.7 124.1 49.2 44 B LEU O 613 175.7 123.4 50.2 44 B LEU N 614 175.5 125.4 49.2 46 B LEU CA 614 175.4 126.2 50.4 48 B LEU CB 614 175.8 127.6 50.2 47 B LEU CG 614 177.2 128.0 49.7 47 B LEU CD1 614 177.2 129.4 49.2 46 B LEU CD2 614 178.1 127.8 50.9 47 B LEU C 614 174.0 126.1 50.9 50 B LEU O 614 173.6 126.8 51.9 50 B ASP N 615 173.2 125.2 50.3 52 B ASP CA 615 171.8 125.1 50.7 55 B ASP CB 615 171.7 124.4 52.1 55 B ASP CG 615 170.3 123.7 52.3 54 B ASP OD1 615 169.4 123.8 51.5 54 B ASP OD2 615 170.2 123.1 53.4 54 B ASP C 615 171.0 126.4 50.7 56 B ASP O 615 170.0 126.5 51.4 58 B GLU N 616 171.5 127.3 49.9 57 B GLU CA 616 170.8 128.6 49.8 59 B GLU CB 616 171.7 129.7 49.5 61 B GLU CG 616 172.9 129.8 50.4 63 B GLU CD 616 172.6 130.3 51.8 64 B GLU OE1 616 171.4 130.6 52.1 65 B GLU OE2 616 173.6 130.5 52.6 65 B GLU C 616 169.8 128.4 48.7 60 B GLU O 616 170.1 127.7 47.7 60 B PRO N 617 168.6 128.9 48.9 61 B PRO CD 617 168.2 129.8 50.0 62 B PRO CA 617 167.4 128.8 47.9 62 B PRO CB 617 166.3 129.4 48.7 63 B PRO CG 617 167.0 130.5 49.5 63 B PRO C 617 167.6 129.6 46.7 62 B PRO O 617 168.3 130.6 46.6 62 B ILE N 618 166.9 129.1 45.6 63 B ILE CA 618 166.9 129.7 44.3 63 B ILE CB 618 167.4 128.6 43.2 63 B ILE CG2 618 167.3 129.2 41.8 63 B ILE CG1 618 168.9 128.2 43.5 62 B ILE CD1 618 169.1 127.1 44.5 62 B ILE C 618 165.5 130.2 44.0 62 B ILE O 618 164.8 129.6 43.1 63 B PRO N 619 165.0 131.2 44.7 60 B PRO CD 619 165.9 132.1 45.5 60 B PRO CA 619 163.7 131.8 44.6 59 B PRO CB 619 164.0 133.3 44.9 60 B PRO CG 619 165.0 133.2 46.0 60 B PRO C 619 163.0 131.7 43.3 59 B PRO O 619 163.4 132.0 42.2 59 B GLN N 620 161.7 131.2 43.4 59 B GLN CA 620 160.9 130.9 42.3 59 B GLN CB 620 159.4 130.7 42.8 61 B GLN CG 620 159.4 129.8 44.1 64 B GLN CD 620 158.0 129.1 44.3 65 B GLN OE1 620 157.0 129.4 43.6 65 B GLN NE2 620 158.0 128.2 45.3 65 B GLN C 620 160.9 132.0 41.2 58 B GLN O 620 161.0 131.6 40.0 58 B ILE N 621 161.0 133.2 41.5 57 B ILE CA 621 161.1 134.3 40.5 56 B ILE CB 621 160.8 135.7 41.2 57 B ILE CG2 621 160.6 136.8 40.1 56 B ILE CG1 621 159.5 135.6 42.0 57 B ILE CD1 621 159.6 135.0 43.4 56 B ILE C 621 162.5 134.5 39.8 54 B ILE O 621 162.6 134.8 38.6 51 B VAL N 622 163.6 134.2 40.6 51 B VAL CA 622 164.9 134.3 40.0 50 B VAL CB 622 166.0 134.3 41.1 49 B VAL CG1 622 166.2 132.9 41.6 49 B VAL CG2 622 167.2 134.9 40.5 50 B VAL C 622 165.0 133.2 39.1 50 B VAL O 622 165.6 133.3 37.9 49 B ALA N 623 164.5 132.0 39.5 49 B ALA CA 623 164.6 130.8 38.7 47 B ALA CB 623 163.9 129.7 39.4 47 B ALA C 623 164.0 131.0 37.3 47 B ALA O 623 164.6 130.7 36.3 47 B THR N 624 162.8 131.6 37.3 47 B THR CA 624 162.1 131.9 36.0 46 B THR CB 624 160.8 132.7 36.3 46 B THR OG1 624 160.0 131.9 37.1 46 B THR CG2 624 160.1 133.0 35.0 44 B THR C 624 163.0 132.8 35.1 47 B THR O 624 163.1 132.6 33.9 48 B ASP N 625 163.6 133.8 35.8 48 B ASP CA 625 164.5 134.7 35.1 47 B ASP CB 625 165.1 135.8 36.0 49 B ASP CG 625 164.0 136.7 36.6 50 B ASP OD1 625 162.9 136.9 35.9 50 B ASP OD2 625 164.1 137.2 37.8 50 B ASP C 625 165.6 133.9 34.4 44 B ASP O 625 165.9 134.0 33.2 44 B VAL N 626 166.3 133.0 35.2 41 B VAL CA 626 167.3 132.2 34.7 40 B VAL CB 626 167.9 131.2 35.7 39 B VAL CG1 626 168.9 130.4 35.1 39 B VAL CG2 626 168.4 131.9 37.0 39 B VAL C 626 166.8 131.5 33.5 41 B VAL O 626 167.4 131.5 32.5 42 B CYS N 627 165.6 130.9 33.7 40 B CYS CA 627 165.0 130.1 32.6 40 B CYS CB 627 163.6 129.5 33.1 39 B CYS SG 627 163.8 128.2 34.3 39 B CYS C 627 164.8 130.9 31.3 40 B CYS O 627 165.1 130.4 30.3 39 B GLN N 628 164.2 132.1 31.5 40 B GLN CA 628 163.9 132.9 30.3 40 B GLN CB 628 163.1 134.1 30.7 42 B GLN CG 628 161.7 133.7 31.1 45 B GLN CD 628 160.8 134.8 31.5 47 B GLN OE1 628 161.0 136.0 31.1 47 B GLN NE2 628 159.8 134.6 32.4 48 B GLN C 628 165.2 133.4 29.7 39 B GLN O 628 165.2 133.5 28.4 38 B PHE N 629 166.2 133.6 30.5 38 B PHE CA 629 167.5 134.0 29.9 37 B PHE CB 629 168.5 134.5 31.0 36 B PHE CG 629 169.9 134.8 30.5 35 B PHE CD1 629 170.1 135.8 29.6 35 B PHE CD2 629 171.0 134.1 31.0 35 B PHE CE1 629 171.4 136.0 29.1 35 B PHE CE2 629 172.3 134.3 30.6 34 B PHE CZ 629 172.5 135.3 29.6 34 B PHE C 629 168.2 132.9 29.1 37 B PHE O 629 168.6 133.1 28.0 37 B LEU N 630 168.3 131.7 29.7 36 B LEU CA 630 168.8 130.5 29.1 35 B LEU CB 630 168.9 129.3 30.0 31 B LEU CG 630 169.9 129.5 31.2 29 B LEU CD1 630 169.8 128.4 32.2 28 B LEU CD2 630 171.3 129.6 30.6 27 B LEU C 630 168.1 130.2 27.8 37 B LEU O 630 168.7 129.6 26.8 38 B GLU N 631 166.8 130.6 27.7 38 B GLU CA 631 166.1 130.4 26.5 40 B GLU CB 631 164.6 130.8 26.7 43 B GLU CG 631 163.8 129.8 27.6 48 B GLU CD 631 162.3 130.0 27.4 51 B GLU OE1 631 161.6 130.6 28.2 51 B GLU OE2 631 161.8 129.6 26.3 52 B GLU C 631 166.6 131.3 25.4 38 B GLU O 631 166.5 130.9 24.2 37 B LEU N 632 167.1 132.5 25.8 37 B LEU CA 632 167.6 133.4 24.8 37 B LEU CB 632 167.7 134.8 25.4 38 B LEU CG 632 166.5 135.5 25.9 38 B LEU CD1 632 166.8 136.7 26.8 39 B LEU CD2 632 165.6 135.9 24.8 39 B LEU C 632 169.0 133.0 24.3 36 B LEU O 632 169.4 133.2 23.2 36 B CYS N 633 169.7 132.3 25.2 35 B CYS CA 633 171.0 131.7 24.9 35 B CYS CB 633 171.7 131.2 26.1 34 B CYS SG 633 172.2 132.6 27.2 34 B CYS C 633 170.8 130.5 23.9 35 B CYS O 633 171.7 130.3 23.1 35 B GLN N 634 169.7 129.8 24.1 35 B GLN CA 634 169.5 128.6 23.3 35 B GLN CB 634 168.2 128.0 23.8 34 B GLN CG 634 167.9 126.7 23.0 34 B GLN CD 634 166.8 125.9 23.7 34 B GLN OE1 634 165.8 126.4 24.1 35 B GLN NE2 634 167.1 124.6 23.9 34 B GLN C 634 169.4 128.9 21.8 35 B GLN O 634 168.8 129.9 21.4 35 B SER N 635 170.0 128.1 21.0 35 B SER CA 635 170.0 128.3 19.6 35 B SER CB 635 171.3 127.7 19.0 34 B SER OG 635 171.3 127.6 17.6 33 B SER C 635 168.8 127.6 18.8 37 B SER O 635 168.3 126.5 19.3 37 B PRO N 636 168.4 128.1 17.7 38 B PRO CD 636 168.9 129.4 17.1 39 B PRO CA 636 167.3 127.5 16.9 40 B PRO CB 636 167.0 128.6 15.9 39 B PRO CG 636 168.4 129.3 15.6 40 B PRO C 636 167.8 126.3 16.2 40 B PRO O 636 167.1 125.7 15.4 41 B ASP N 637 169.1 125.9 16.5 42 B ASP CA 637 169.7 124.7 15.9 41 B ASP CB 637 170.9 125.1 15.1 44 B ASP CG 637 170.5 126.0 14.0 48 B ASP OD1 637 169.4 125.9 13.4 49 B ASP OD2 637 171.3 126.9 13.7 48 B ASP C 637 170.1 123.7 17.1 39 B ASP O 637 170.8 122.8 16.8 41 B GLY N 638 169.5 124.0 18.3 37 B GLY CA 638 169.9 123.1 19.4 33 B GLY C 638 171.1 123.6 20.1 31 B GLY O 638 172.0 124.2 19.5 32 B GLY N 639 171.2 123.3 21.4 30 B GLY CA 639 172.4 123.7 22.1 29 B GLY C 639 172.3 125.2 22.5 29 B GLY O 639 171.4 125.9 22.0 28 B PHE N 640 173.2 125.6 23.4 29 B PHE CA 640 173.2 127.0 23.9 28 B PHE CB 640 172.9 127.0 25.4 28 B PHE CG 640 171.7 126.3 25.8 29 B PHE CD1 640 171.6 124.9 25.9 30 B PHE CD2 640 170.5 127.0 26.2 30 B PHE CE1 640 170.4 124.2 26.2 30 B PHE CE2 640 169.3 126.3 26.5 31 B PHE CZ 640 169.3 124.9 26.5 31 B PHE C 640 174.4 127.7 23.6 28 B PHE O 640 175.5 127.1 23.7 29 B GLY N 641 174.3 129.0 23.4 28 B GLY CA 641 175.5 129.8 23.1 27 B GLY C 641 176.0 130.4 24.4 26 B GLY O 641 175.3 130.2 25.5 27 B GLY N 642 177.1 131.2 24.4 26 B GLY CA 642 177.6 131.8 25.6 26 B GLY C 642 176.8 133.0 26.1 27 B GLY O 642 177.1 133.6 27.1 28 B GLY N 643 175.8 133.4 25.3 27 B GLY CA 643 175.1 134.6 25.6 26 B GLY C 643 174.0 134.7 24.6 28 B GLY O 643 174.0 133.9 23.6 28 B PRO N 644 172.9 135.5 24.8 29 B PRO CD 644 172.7 136.5 25.9 29 B PRO CA 644 171.9 135.6 23.8 30 B PRO CB 644 171.1 136.8 24.3 29 B PRO CG 644 171.2 136.7 25.8 28 B PRO C 644 172.4 135.9 22.4 31 B PRO O 644 173.3 136.8 22.3 33 B GLY N 645 172.0 135.1 21.5 33 B GLY CA 645 172.4 135.2 20.1 33 B GLY C 645 173.7 134.7 19.6 34 B GLY O 645 174.2 134.9 18.5 34 B GLN N 646 174.4 133.9 20.5 32 B GLN CA 646 175.7 133.3 20.1 32 B GLN CB 646 176.6 133.4 21.3 32 B GLN CG 646 177.0 134.8 21.8 31 B GLN CD 646 177.8 134.8 23.1 31 B GLN OE1 646 177.6 135.7 23.9 32 B GLN NE2 646 178.7 133.8 23.3 31 B GLN C 646 175.5 131.9 19.6 32 B GLN O 646 174.6 131.2 20.1 33 B TYR N 647 176.3 131.5 18.7 30 B TYR CA 647 176.2 130.1 18.1 28 B TYR CB 647 177.4 129.9 17.2 28 B TYR CG 647 177.4 130.8 16.0 2B B TYR CD1 647 178.5 131.0 15.2 28 B TYR CE1 647 178.5 131.8 14.1 29 B TYR CD2 647 176.2 131.6 15.7 27 B TYR CE2 647 176.2 132.4 14.7 27 B TYR CZ 647 177.3 132.5 13.8 28 B TYR OH 647 177.3 133.3 12.7 31 B TYR C 647 176.4 129.2 19.3 28 B TYR O 647 177.0 129.5 20.3 29 B PRO N 648 175.7 128.0 19.2 27 B PRO CD 648 174.9 127.5 18.1 27 B PRO CA 648 175.8 127.1 20.3 25 B PRO CB 648 174.7 126.1 20.0 25 B PRO CG 648 174.7 126.0 18.5 27 B PRO C 648 177.2 126.4 20.4 24 B PRO O 648 177.8 126.2 19.4 25 B HIS N 649 177.6 126.2 21.7 21 B HIS CA 649 178.9 125.6 22.0 21 B HIS CB 649 179.8 126.8 22.4 19 B HIS CG 649 181.2 126.4 22.7 17 B HIS CD2 649 182.3 126.8 22.1 17 B HIS ND1 649 181.6 125.7 23.8 17 B HIS CE1 649 182.9 125.7 23.9 16 B HIS NE2 649 183.4 126.3 22.8 17 B HIS C 649 178.6 124.6 23.1 23 B HIS O 649 177.7 124.8 23.9 24 B LEU N 650 179.3 123.5 23.0 23 B LEU CA 650 179.0 122.4 24.0 23 B LEU CB 650 179.8 121.1 23.7 22 B LEU CG 650 179.2 120.1 22.7 21 B LEU CD1 650 180.1 119.0 22.5 21 B LEU CD2 650 177.9 119.6 23.3 20 B LEU C 650 179.2 122.8 25.5 25 B LEU O 650 178.5 122.3 26.3 26 B ALA N 651 180.2 123.6 25.8 23 B ALA CA 651 180.5 124.0 27.2 22 B ALA CB 651 181.8 124.7 27.4 22 B ALA C 651 179.3 124.9 27.7 23 B ALA O 651 178.8 124.6 28.8 24 B PRO N 652 178.9 125.9 27.0 23 B PRO CD 652 179.7 126.7 26.0 23 B PRO CA 652 177.7 126.7 27.4 23 B PRO CB 652 177.6 127.8 26.4 23 B PRO CG 652 179.1 128.1 26.2 21 B PRO C 652 176.5 125.8 27.5 25 B PRO O 652 175.6 126.0 28.3 27 B THR N 653 176.4 124.8 26.6 25 B THR CA 653 175.3 123.8 26.6 23 B THR CB 653 175.3 122.9 25.3 24 B THR OG1 653 175.2 123.7 24.2 25 B THR CG2 653 174.2 121.9 25.4 24 B THR C 653 175.3 123.0 27.8 23 B THR O 653 174.2 122.7 28.5 24 B TYR N 654 176.4 122.4 28.2 22 B TYR CA 654 176.5 121.6 29.4 22 B TYR CB 654 177.9 121.2 29.6 22 B TYR CG 654 178.2 120.7 31.0 21 B TYR CD1 654 178.0 119.3 31.4 20 B TYR CE1 654 178.4 118.9 32.7 20 B TYR CD2 654 178.9 121.5 32.0 21 B TYR CE2 654 179.2 121.0 33.2 21 B TYR CZ 654 179.0 119.7 33.6 21 B TYR OH 654 179.4 119.3 34.8 21 B TYR C 654 176.0 122.5 30.6 24 B TYR O 654 175.2 122.1 31.4 24 B ALA N 655 176.6 123.7 30.7 25 B ALA CA 655 176.3 124.7 31.7 25 B ALA CB 655 177.1 125.9 31.5 24 B ALA C 655 174.8 125.0 31.8 25 B ALA O 655 174.2 125.0 32.8 26 B ALA N 656 174.2 125.3 30.6 26 B ALA CA 656 172.8 125.6 30.6 26 B ALA CB 656 172.4 126.0 29.2 24 B ALA C 656 172.0 124.5 31.1 28 B ALA O 656 171.2 124.6 32.1 29 B VAL N 657 172.1 123.3 30.4 29 B VAL CA 657 171.4 122.1 30.8 29 B VAL CB 657 171.8 120.9 29.9 29 B VAL CG1 657 171.1 119.6 30.4 29 B VAL CG2 657 171.3 121.2 28.5 27 B VAL C 657 171.6 121.8 32.3 29 B VAL O 657 170.6 121.6 33.0 31 B ASN N 658 172.8 121.8 32.9 30 B ASN CA 658 173.0 121.6 34.3 29 B ASN CB 658 174.5 121.6 34.7 29 B ASN CG 658 175.1 120.3 34.9 30 B ASN OD1 658 174.6 119.3 34.4 32 B ASN ND2 658 176.2 120.2 35.7 31 B ASN C 658 172.3 122.6 35.2 30 B ASN O 658 171.7 122.2 36.2 30 B ALA N 659 172.3 123.9 34.8 30 B ALA CA 659 171.7 124.9 35.5 29 B ALA CB 659 171.9 126.3 34.8 28 B ALA C 659 170.2 124.6 35.5 30 B ALA O 659 169.6 124.5 36.6 31 B LEU N 660 169.6 124.5 34.3 31 B LEU CA 660 168.1 124.2 34.2 32 B LEU CB 660 167.8 123.9 32.7 30 B LEU CG 660 167.8 125.1 31.8 30 B LEU CD1 660 167.5 124.7 30.4 30 B LEU CD2 660 166.8 126.2 32.3 30 B LEU C 660 167.7 123.0 35.1 33 B LEU O 660 166.6 122.9 35.7 34 B CYS N 661 168.6 122.0 35.2 34 B CYS CA 661 168.4 120.9 36.0 36 B CYS CB 661 169.4 119.7 35.7 35 B CYS SG 661 168.9 118.8 34.2 33 B CYS C 661 168.4 121.2 37.5 38 B CYS O 661 167.7 120.5 38.3 39 B ILE N 662 169.3 122.1 38.0 40 B ILE CA 662 169.4 122.4 39.4 40 B ILE CB 662 170.6 123.3 39.7 41 B ILE CG2 662 170.7 123.6 41.2 42 B ILE CG1 662 171.9 122.7 39.2 41 B ILE CD1 662 173.1 123.5 39.5 41 B ILE C 662 168.1 123.1 39.8 40 B ILE O 662 167.6 122.9 40.9 40 B ILE N 663 167.5 123.9 38.8 39 B ILE CA 663 166.2 124.5 39.1 39 B ILE CB 663 166.0 125.6 38.0 37 B ILE CG2 663 164.6 126.2 38.1 37 B ILE CG1 663 167.0 126.7 38.1 36 B ILE CD1 663 166.9 127.8 37.0 34 B ILE C 663 165.1 123.5 39.1 41 B ILE O 663 164.1 123.6 39.7 42 B CLY N 664 165.3 122.3 38.4 40 B GLY CA 664 164.4 121.3 38.4 41 B GLY C 664 162.9 121.5 38.2 41 B GLY O 664 162.1 120.6 38.6 42 B THR N 665 162.4 122.6 37.7 41 B THR CA 665 161.0 122.8 37.5 42 B THR CB 665 160.6 124.3 37.7 41 B THR OG1 665 160.9 125.0 36.5 41 B THR CG2 665 161.3 125.0 38.8 41 B THR C 665 160.6 122.4 36.2 43 B THR O 665 161.4 122.3 35.3 42 B GLU N 666 159.3 122.1 36.0 46 B GLU CA 666 158.8 121.7 34.7 48 B GLU CB 666 157.3 121.2 34.8 50 B GLU CG 666 157.2 119.7 35.0 53 B GLU CD 666 157.9 119.1 36.3 54 B GLU OE1 666 158.0 119.9 37.2 56 B GLU OE2 666 158.2 117.9 36.3 55 B GLU C 666 159.0 122.8 33.7 49 B GLU O 666 158.9 122.6 32.5 50 B GLU N 667 159.2 124.0 34.2 48 B GLU CA 667 159.5 125.2 33.4 47 B GLU CB 667 159.2 126.5 34.1 48 B GLU CG 667 159.5 127.7 33.3 50 B GLU CD 667 159.7 129.0 34.1 51 B GLU OE1 667 159.9 128.9 35.4 51 B GLU OE2 667 159.8 130.1 33.6 52 B GLU C 667 160.9 125.2 32.9 45 B GLU O 667 161.2 125.5 31.7 45 B ALA N 668 161.8 124.8 33.8 42 B ALA CA 668 163.2 124.7 33.4 40 B ALA CB 668 164.0 124.3 34.7 40 B ALA C 668 163.4 123.6 32.4 39 B ALA O 668 163.8 123.8 31.3 38 B TYR N 669 162.9 122.4 32.7 37 B TYR CA 669 163.0 121.2 31.8 35 B TYR CB 669 162.3 120.0 32.4 34 B TYR CG 669 162.7 119.5 33.7 32 B TYR CD1 669 161.8 119.0 34.6 31 B TYR CE1 669 162.2 118.5 35.9 30 B TYR CD2 669 164.1 119.5 34.1 31 B TYR CE2 669 164.5 119.0 35.4 31 B TYR CZ 669 163.5 118.5 36.2 30 B TYR OH 669 163.9 118.0 37.5 28 B TYR C 669 162.4 121.6 30.5 36 B TYR O 669 163.0 121.2 29.4 37 B ASN N 670 161.3 122.3 30.5 36 B ASN CA 670 160.7 122.6 29.2 37 B ASN CB 670 159.3 123.2 29.4 39 B ASN CG 670 158.3 122.0 29.7 39 B ASN OD1 670 158.6 121.0 30.2 39 B ASN ND2 670 157.0 122.3 29.4 40 B ASN C 670 161.5 123.6 28.3 37 B ASN O 670 161.2 123.8 27.2 38 B VAL N 671 162.5 124.2 28.9 36 B VAL CA 671 163.3 125.2 28.2 36 B VAL CB 671 164.3 125.9 29.1 36 B VAL CG1 671 165.2 126.7 28.2 36 B VAL CG2 671 163.5 126.7 30.1 36 B VAL C 671 164.0 124.4 27.1 36 B VAL O 671 164.2 124.9 25.9 36 B ILE N 672 164.6 123.3 27.4 35 B ILE CA 672 165.4 122.5 26.5 34 B ILE CB 672 166.1 121.3 27.3 32 B ILE CG2 672 167.1 120.6 26.4 31 B ILE CG1 672 166.8 121.8 28.6 30 B ILE CD1 672 167.3 120.7 29.5 28 B ILE C 672 164.7 121.8 25.4 35 B ILE O 672 163.7 121.1 25.6 36 B ASN N 673 165.1 122.2 24.1 35 B ASN CA 673 164.5 121.6 22.9 37 B ASN CB 673 164.6 122.6 21.8 37 B ASN CG 673 164.1 122.1 20.5 39 B ASN OD1 673 164.2 121.0 20.2 40 B ASN ND2 673 163.4 123.0 19.7 39 B ASN C 673 165.2 120.4 22.6 38 B ASN O 673 166.3 120.4 21.9 39 B ARG N 674 164.7 119.2 23.0 40 B ARG CA 674 165.4 118.0 22.8 40 B ARG CB 674 164.7 116.9 23.7 39 B ARG CG 674 164.7 117.2 25.1 39 B ARG CD 674 163.8 116.3 25.9 40 B ARG NE 674 164.1 114.8 25.7 41 B ARG CZ 674 163.6 114.0 24.9 42 B ARG NH1 674 162.5 114.4 24.1 42 B ARG NH2 674 163.9 112.7 24.9 42 B ARG C 674 165.6 117.4 21.4 41 B ARG O 674 166.7 116.9 21.1 41 B GLU N 675 164.6 117.6 20.6 43 B GLU CA 675 164.8 117.1 19.2 45 B GLU CB 675 163.5 117.2 18.4 49 B GLU CG 675 162.4 118.2 19.0 55 B GLU CD 675 161.7 117.8 20.3 57 B GLU OE1 675 161.9 118.5 21.3 58 B GLU OE2 675 161.0 116.7 20.3 59 B GLU C 675 165.9 117.8 18.5 45 B GLU O 675 166.7 117.3 17.7 44 B LYS N 676 166.1 119.1 18.9 43 B LYS CA 676 167.2 119.9 18.3 41 B LYS CB 676 166.7 121.4 18.1 43 B LYS CG 676 166.2 121.5 16.6 46 B LYS CD 676 166.0 123.0 16.3 49 B LYS CE 676 164.9 123.6 17.0 51 B LYS NZ 676 164.6 125.0 16.7 52 B LYS C 676 168.5 119.8 19.0 38 B LYS O 676 169.5 120.0 18.4 37 B LEU N 677 168.4 119.5 20.3 35 B LEU CA 677 169.7 119.3 21.1 33 B LEU CB 677 169.4 119.0 22.5 31 B LEU CG 677 170.5 118.7 23.5 30 B LEU CD1 677 171.6 119.8 23.2 31 B LEU CD2 677 170.1 118.7 24.9 30 B LEU C 677 170.4 118.1 20.4 33 B LEU O 677 171.6 118.3 20.1 33 B LEU N 678 169.7 117.0 20.2 35 B LEU CA 678 170.2 115.8 19.5 34 B LEU CB 678 169.1 114.8 19.4 35 B LEU CG 678 169.3 113.3 19.3 36 B LEU CD1 678 168.5 112.7 18.2 36 B LEU CD2 678 170.8 113.0 19.1 37 B LEU C 678 170.8 116.1 18.2 34 B LEU O 678 171.9 115.7 17.8 34 B GLN N 679 170.0 116.9 17.4 34 B GLN CA 679 170.3 117.3 16.1 36 B GLN CB 679 169.3 118.3 15.5 39 B GLN CG 679 169.5 118.9 14.2 43 B GLN CD 679 168.3 119.6 13.6 46 B GLN OE1 679 168.3 120.8 13.4 4B B GLN NE2 679 167.2 118.8 13.4 46 B GLN C 679 171.7 118.0 16.1 35 B GLN O 679 172.5 117.7 15.2 35 B TYR N 680 171.9 118.8 17.1 34 B TYR CA 680 173.1 119.6 17.3 31 B TYR CB 680 172.9 120.5 18.5 30 B TYR CG 680 174.1 121.3 18.9 29 B TYR CD1 680 174.7 122.2 17.9 28 B TYR CE1 680 175.9 122.9 18.2 28 B TYR CD2 680 174.7 121.3 20.1 28 B TYR CE2 680 175.8 122.0 20.4 27 B TYR CZ 680 176.4 122.8 19.5 27 B TYR OH 680 177.6 123.4 19.8 29 B TYR C 680 174.3 118.6 17.6 29 B TYR O 680 175.3 118.7 17.0 29 B LEU N 681 174.1 117.7 18.6 27 B LEU CA 681 175.2 116.8 19.0 27 B LEU CB 681 174.7 115.8 20.1 26 B LEU CG 681 174.3 116.5 21.4 26 B LEU CD1 681 174.0 115.4 22.5 25 B LEU CD2 681 175.4 117.3 21.9 25 B LEU C 681 175.6 116.0 17.8 27 B LEU O 681 176.8 115.8 17.6 26 B TYR N 682 174.7 115.6 16.9 28 B TYR CA 682 175.0 114.9 15.8 29 B TYR CB 682 173.8 114.4 15.0 31 B TYR CG 682 173.3 113.0 15.3 32 B TYR CD1 682 172.0 112.8 15.8 32 B TYR CE1 682 171.6 111.5 16.1 32 B TYR CD2 682 174.2 111.9 15.2 32 B TYR CE2 682 173.7 110.6 15.5 32 B TYR CZ 682 172.4 110.4 15.9 33 B TYR OH 682 172.0 109.2 16.2 33 B TYR C 682 175.9 115.8 14.8 29 B TYR O 682 176.8 115.3 14.2 30 B SER N 683 175.6 117.1 14.8 30 B SER CA 683 176.4 118.0 13.9 29 B SER CB 683 175.7 119.4 13.8 30 B SER OG 683 175.9 120.2 15.0 30 B SER C 683 177.8 118.2 14.4 29 B SER O 683 178.6 118.7 13.6 29 B LEU N 684 178.1 117.7 15.6 28 B LEU CA 684 179.5 117.9 16.1 27 B LEU CB 684 179.4 118.4 17.5 24 B LEU CG 684 178.6 119.7 17.7 23 B LEU CD1 684 178.7 120.1 19.2 22 B LEU CD2 684 179.1 120.8 16.8 20 B LEU C 684 180.3 116.5 16.1 27 B LEU O 684 181.5 116.5 16.0 29 B LYS N 685 179.5 115.4 16.1 27 B LYS CA 685 180.1 114.1 16.0 26 B LYS CB 685 179.0 113.0 15.8 27 B LYS CG 685 179.1 111.8 16.7 27 B LYS CD 685 180.5 111.3 16.8 27 B LYS CE 685 180.6 110.0 17.7 28 B LYS NZ 685 179.9 108.9 17.1 27 B LYS C 685 181.1 114.0 14.9 27 B LYS O 685 180.9 114.4 13.8 26 B GLN N 686 182.3 113.3 15.2 27 B GLN CA 686 183.3 113.1 14.3 28 B GLN CB 686 184.7 113.6 14.9 28 B GLN CG 686 184.7 115.1 15.1 28 B GLN CD 686 184.6 115.8 13.9 30 B GLN OE1 686 185.5 115.8 13.0 32 B GLN NE2 686 183.4 116.4 13.7 30 B GLN C 686 183.5 111.6 14.1 29 B GLN O 686 183.1 110.8 14.9 30 B PRO N 687 184.0 111.2 12.9 30 B PRO CD 687 184.4 112.1 11.8 30 B PRO CA 687 184.2 109.8 12.5 29 B PRO CB 687 184.8 110.0 11.1 30 B PRO CG 687 184.3 111.2 10.6 31 B PRO C 687 185.1 109.1 13.5 29 B PRO O 687 184.9 107.9 13.7 29 B ASP N 688 186.1 109.8 14.0 28 B ASP CA 688 187.0 109.1 15.0 27 B ASP CB 688 188.3 109.8 15.1 27 B ASP CG 688 188.3 111.1 15.7 28 B ASP OD1 688 187.2 111.6 16.1 28 B ASP OD2 688 189.4 111.7 15.8 29 B ASP C 688 186.3 108.9 16.3 26 B ASP O 688 186.9 108.4 17.3 28 B GLY N 689 185.1 109.4 16.5 23 B GLY CA 689 184.4 109.3 17.8 23 B GLY C 689 184.4 110.5 18.6 22 B GLY O 689 183.6 110.6 19.5 22 B SER N 690 185.2 111.5 18.3 22 B SER CA 690 185.2 112.8 19.0 20 B SER CB 690 186.5 113.5 18.9 20 B SER OG 690 186.8 113.7 17.5 18 B SER C 690 184.0 113.7 18.6 21 B SER O 690 183.2 113.3 17.8 23 B PHE N 691 183.9 114.8 19.3 22 B PHE CA 691 182.9 115.8 19.0 19 B PHE CB 691 181.9 115.9 20.1 19 B PHE CG 691 180.9 114.8 20.2 19 B PHE CD1 691 181.2 113.6 21.0 19 B PHE CD2 691 179.7 114.8 19.6 19 B PHE CE1 691 180.3 112.6 21.1 19 B PHE CE2 691 178.7 113.8 19.7 18 B PHE CZ 691 179.0 112.7 20.5 18 B PHE C 691 183.6 117.2 18.9 19 B PHE O 691 184.6 117.4 19.6 18 B LEU N 692 183.1 118.1 18.1 20 B LEU CA 692 183.7 119.4 18.0 21 B LEU CB 692 183.3 120.1 16.8 21 B LEU CG 692 183.6 119.5 15.4 20 B LEU CD1 692 182.8 120.3 14.4 20 B LEU CD2 692 185.1 119.4 15.1 18 B LEU C 692 183.1 120.1 19.3 23 B LEU O 692 182.1 119.6 19.8 23 B MET N 693 183.7 121.2 19.7 23 B MET CA 693 183.1 121.9 20.8 22 B MET CB 693 184.1 122.9 21.5 21 B MET CG 693 185.2 122.1 22.4 22 B MET SD 693 184.4 121.2 23.7 25 B MET CE 693 183.8 122.4 24.8 23 B MET C 693 182.0 122.8 20.3 22 B MET O 693 181.0 123.1 21.0 21 B HIS N 694 182.1 123.1 19.0 22 B HIS CA 694 181.0 123.9 18.3 23 B HIS CB 694 181.0 125.3 18.7 22 B HIS CG 694 182.2 126.1 18.5 22 B HIS CD2 694 183.4 126.1 19.1 20 B HIS ND1 694 182.3 127.1 17.5 22 B HIS CE1 694 183.5 127.6 17.5 21 B HIS NE2 694 184.2 127.0 18.5 21 B HIS C 694 181.4 123.8 16.8 25 B HIS O 694 182.5 123.3 16.4 26 B VAL N 695 180.5 124.2 15.9 25 B VAL CA 695 180.7 124.1 14.5 25 B VAL CB 695 179.5 124.5 13.7 26 B VAL CG1 695 179.8 124.7 12.2 26 B VAL CG2 695 178.3 123.5 13.9 25 B VAL C 695 181.9 125.0 14.1 26 B VAL O 695 181.9 126.2 14.3 28 B GLY N 696 182.9 124.4 13.5 26 B GLY CA 696 184.1 125.1 13.1 26 B GLY C 696 185.0 125.2 14.2 26 B GLY O 696 186.1 125.8 14.1 26 B GLY N 697 184.6 124.6 15.4 24 B GLY CA 697 185.5 124.7 16.6 22 B GLY C 697 186.5 123.6 16.8 22 B GLY O 697 186.7 122.7 16.0 23 B GLU N 698 187.1 123.6 18.0 20 B GLU CA 698 188.1 122.7 18.4 20 B GLU CB 698 189.1 123.4 19.4 20 B GLU CG 698 188.7 123.6 20.8 21 B GLU CD 698 187.7 124.8 21.0 22 B GLU OE1 698 187.4 125.6 20.1 22 B GLU OE2 698 187.4 125.0 22.2 22 B GLU C 698 187.6 121.4 19.0 19 B GLU O 698 186.4 121.3 19.3 19 B VAL N 699 188.4 120.4 19.0 19 B VAL CA 699 188.1 119.0 19.6 18 B VAL CB 699 188.3 117.9 18.5 17 B VAL CG1 699 188.2 116.5 19.2 16 B VAL CG2 699 187.2 118.0 17.4 18 B VAL C 699 189.0 118.7 20.7 18 B VAL O 699 190.2 118.8 20.6 18 B ASP N 700 188.5 118.3 21.9 18 B ASP CA 700 189.3 117.8 23.0 19 B ASP CB 700 190.1 118.9 23.7 20 B ASP CG 700 189.3 120.0 24.3 22 B ASP OD1 700 188.4 119.7 25.1 22 B ASP OD2 700 189.5 121.1 23.9 22 B ASP C 700 188.2 117.1 23.9 19 B ASP O 700 187.0 117.2 23.7 19 B VAL N 701 188.7 116.3 24.9 20 B VAL CA 701 187.7 115.6 25.8 20 B VAL CB 701 188.3 114.8 27.0 20 B VAL CG1 701 188.1 113.3 26.8 18 B VAL CG2 701 189.7 115.1 27.2 20 B VAL C 701 186.6 116.3 26.4 21 B VAL O 701 185.6 115.7 26.7 23 B ARG N 702 186.7 117.6 26.5 22 B ARG CA 702 185.6 118.4 27.2 22 B ARG CB 702 185.8 119.9 27.2 21 B ARG CG 702 187.0 120.4 28.1 19 B ARG CD 702 187.3 121.9 27.8 19 B ARG NE 702 187.6 122.1 26.4 19 B ARG CZ 702 187.4 123.2 25.6 18 B ARG NH1 702 187.8 123.3 24.4 17 B ARG NH2 702 186.7 124.2 26.1 18 B ARG C 702 184.3 118.1 26.4 24 B ARG O 702 183.2 118.0 27.0 25 B SER N 703 184.4 118.0 25.1 25 B SER CA 703 183.2 117.8 24.2 25 B SER CB 703 183.6 117.9 22.8 26 B SER OG 703 184.3 116.8 22.3 25 B SER C 703 182.5 116.5 24.5 26 B SER O 703 181.3 116.4 24.5 27 B ALA N 704 183.3 115.4 24.7 26 B ALA CA 704 182.8 114.1 25.0 26 B ALA CB 704 183.9 113.1 25.1 26 B ALA C 704 181.9 114.0 26.2 27 B ALA O 704 180.9 113.4 26.2 28 B TYR N 705 182.4 114.7 27.3 27 B TYR CA 705 181.7 114.8 28.6 27 B TYR CB 705 182.7 115.4 29.6 27 B TYR CG 705 182.1 115.7 30.9 27 B TYR CD1 705 181.4 114.8 31.7 27 B TYR CE1 705 180.8 115.1 32.9 28 B TYR CD2 705 182.1 117.0 31.4 27 B TYR CE2 705 181.5 117.4 32.6 28 B TYR CZ 705 180.9 116.4 33.4 28 B TYR OH 705 180.3 116.8 34.6 28 B TYR C 705 180.5 115.8 28.5 26 B TYR O 705 179.4 115.4 29.0 24 B CYS N 706 180.7 117.0 27.9 25 B CYS CA 706 179.5 117.9 27.8 26 B CYS CB 706 180.0 119.1 27.0 26 B CYS SG 706 181.1 120.2 27.9 25 B CYS C 706 178.4 117.2 27.0 27 B CYS O 706 177.3 117.2 27.5 28 B ALA N 707 178.7 116.5 25.9 26 B ALA CA 707 177.7 115.8 25.1 24 B ALA CB 707 178.4 115.3 23.8 22 B ALA C 707 177.1 114.6 25.9 23 B ALA O 707 175.9 114.5 26.0 23 B ALA N 708 177.9 113.8 26.5 24 B ALA CA 708 177.4 112.6 27.3 24 B ALA CB 708 178.5 111.7 27.7 23 B ALA C 708 176.6 113.0 28.5 26 B ALA O 708 175.8 112.2 28.9 27 B SER N 709 176.8 114.2 29.0 27 B SER CA 709 176.1 114.7 30.2 27 B SER CB 709 176.9 115.9 30.9 27 B SER OG 709 176.2 116.4 32.0 27 B SER C 709 174.7 115.2 29.8 28 B SER O 709 173.8 114.9 30.4 28 B VAL N 710 174.7 116.1 28.8 29 B VAL CA 710 173.4 116.6 28.3 29 B VAL CB 710 173.6 117.8 27.4 28 B VAL CG1 710 174.4 118.9 28.1 28 B VAL CG2 710 174.2 117.4 26.1 27 B VAL C 710 172.5 115.6 27.6 29 B VAL O 710 171.3 115.5 27.9 29 B ALA N 711 173.1 114.7 26.8 30 B ALA CA 711 172.3 113.7 26.1 30 B ALA CB 711 173.1 113.0 25.1 28 B ALA C 711 171.7 112.7 27.1 30 B ALA O 711 170.6 112.2 26.9 31 B SER N 712 172.5 112.3 28.1 31 B SER CA 712 172.0 111.3 29.1 33 B SER CB 712 173.1 110.8 30.0 34 B SER OG 712 173.8 111.8 30.7 35 B SER C 712 170.9 111.9 29.9 33 B SER O 712 169.8 111.3 30.0 34 B LEU N 713 171.2 113.1 30.5 33 B LEU CA 713 170.2 113.8 31.4 32 B LEU CB 713 170.7 115.2 31.8 31 B LEU CG 713 171.7 115.1 33.0 30 B LEU CD1 713 172.3 116.5 33.2 29 B LEU CD2 713 171.1 114.6 34.3 29 B LEU C 713 168.9 114.0 30.6 34 B LEU O 713 167.8 113.8 31.2 34 B THR N 714 168.9 114.4 29.4 35 B THR CA 714 167.7 114.6 28.6 35 B THR CB 714 167.9 115.8 27.6 34 B THR OG1 714 169.0 115.6 26.7 34 B THR CG2 714 168.2 117.1 28.4 32 B THR C 714 167.2 113.4 27.9 36 B THR O 714 166.2 113.5 27.1 37 B ASN N 715 167.8 112.2 28.1 36 B ASN CA 715 167.4 111.0 27.4 35 B ASN CB 715 166.0 110.6 28.1 36 B ASN CG 715 165.4 109.4 27.5 37 B ASN OD1 715 166.0 108.3 27.2 38 B ASN ND2 715 164.1 109.5 27.2 37 B ASN C 715 167.2 111.1 25.9 34 B ASN O 715 166.2 110.9 25.3 34 B ILE N 716 168.3 111.5 25.3 31 B ILE CA 716 168.3 111.7 23.8 29 B ILE CB 716 168.5 113.1 23.3 29 B ILE CG2 716 167.4 114.0 23.8 28 B ILE CG1 716 169.8 113.7 23.9 30 B ILE CD1 716 170.3 115.0 23.3 30 B ILE C 716 169.4 110.8 23.2 29 B ILE O 716 169.7 111.0 22.1 28 B ILE N 717 169.9 109.9 24.0 29 B ILE CA 717 170.9 109.0 23.5 32 B ILE CB 717 171.6 108.3 24.7 31 B ILE CG2 717 172.7 107.3 24.2 31 B ILE CG1 717 172.3 109.3 25.6 31 B ILE CD1 717 173.2 108.7 26.7 30 B ILE C 717 170.4 107.9 22.6 33 B ILE O 717 169.7 107.0 23.0 34 B THR N 718 170.7 108.1 21.3 35 B THR CA 718 170.3 107.1 20.3 35 B THR CB 718 170.3 107.8 18.9 35 B THR OG1 718 171.6 108.2 18.5 36 B THR CG2 718 169.3 109.0 18.9 35 B THR C 718 171.4 106.0 20.3 38 B THR O 718 172.3 106.0 21.1 38 B PRO N 719 171.2 105.0 19.4 39 B PRO CD 719 170.0 104.8 18.5 40 B PRO CA 719 172.2 103.9 19.3 39 B PRO CB 719 171.5 103.0 18.3 40 B PRO CG 719 170.0 103.3 18.5 40 B PRO C 719 173.6 104.2 18.8 39 B PRO O 719 174.6 103.7 19.4 38 B ASP N 720 173.7 105.0 17.8 38 B ASP CA 720 175.0 105.4 17.2 39 B ASP CB 720 174.9 105.4 15.7 40 B ASP CG 720 173.9 106.5 15.2 41 B ASP OD1 720 174.0 106.9 14.0 43 B ASP OD2 720 173.1 106.9 16.0 41 B ASP C 720 175.6 106.7 17.7 38 B ASP O 720 176.7 107.1 17.2 37 B LEU N 721 174.9 107.5 18.5 37 B LEU CA 721 175.4 108.8 19.0 35 B LEU CB 721 174.4 109.4 20.1 34 B LEU CG 721 174.9 110.8 20.5 33 B LEU CD1 721 175.1 111.7 19.3 31 B LEU CD2 721 173.9 111.3 21.5 31 B LEU C 721 176.8 108.7 19.5 36 B LEU O 721 177.7 109.4 19.0 36 B PHE N 722 177.1 107.9 20.5 35 B PHE CA 722 178.4 107.8 21.0 36 B PHE CB 722 178.3 107.8 22.6 36 B PHE CG 722 177.7 109.0 23.1 36 B PHE CD1 722 176.4 109.0 23.7 36 B PHE CD2 722 178.3 110.3 23.0 37 B PHE CE1 722 175.8 110.1 24.2 36 B PHE CE2 722 177.6 111.4 23.4 37 B PHE CZ 722 176.4 111.3 24.0 36 B PHE C 722 179.2 106.7 20.5 36 B PHE O 722 180.1 106.1 21.2 36 B GLU N 723 178.9 106.3 19.3 37 B GLU CA 723 179.6 105.2 18.6 37 B GLU CB 723 179.1 105.0 17.2 41 B GLU CG 723 179.2 103.5 16.8 45 B GLU CD 723 178.9 102.6 18.0 48 B GLU OE1 723 177.7 102.7 18.5 49 B GLU OE2 723 179.8 101.9 18.5 49 B GLU C 723 181.1 105.6 18.5 34 B GLU O 723 181.4 106.6 17.9 34 B GLY N 724 181.9 104.8 19.2 32 B GLY CA 724 183.3 105.1 19.1 31 B GLY C 724 183.9 106.1 20.0 28 B GLY O 724 185.1 106.3 20.0 28 B THR N 725 183.1 106.8 20.8 28 B THR CA 725 183.6 107.9 21.6 28 B THR CB 725 182.7 109.1 21.9 29 B THR OG1 725 182.2 109.1 23.3 31 B THR CG2 725 181.5 109.0 21.0 27 B THR C 725 184.3 107.3 22.9 27 B THR O 725 185.3 107.9 23.3 28 B ALA N 726 183.9 106.2 23.3 25 B ALA CA 726 184.6 105.6 24.5 25 B ALA CB 726 183.8 104.3 24.9 25 B ALA C 726 186.0 105.2 24.0 26 B ALA O 726 186.9 105.3 24.8 27 B GLU N 727 186.1 104.8 22.8 25 B GLU CA 727 187.4 104.3 22.2 24 B GLU CB 727 187.2 103.6 20.9 25 B GLU CG 727 186.7 102.1 21.1 26 B GLU CD 727 185.2 101.9 21.3 26 B GLU OE1 727 184.7 100.8 21.7 27 B GLU OE2 727 184.4 102.8 21.0 27 B GLU C 727 188.3 105.5 22.0 23 B GLU O 727 189.4 105.5 22.3 23 B TRP N 728 187.7 106.6 21.5 21 B TRP CA 728 188.5 107.8 21.3 21 B TRP CB 728 187.7 108.9 20.6 21 B TRP CG 728 188.5 110.1 20.3 20 B TRP CD2 728 188.7 111.2 21.1 21 B TRP CE2 728 189.6 112.1 20.4 21 B TRP CE3 728 188.2 111.7 22.3 21 B TRP CD1 728 189.2 110.2 19.2 20 B TRP NE1 728 189.9 111.4 19.2 21 B TRP CZ2 728 190.0 113.3 20.8 21 B TRP CZ3 728 188.7 112.9 22.8 21 B TRP CH2 728 189.5 113.7 22.1 21 B TRP C 728 189.0 108.3 22.6 22 B TRP O 728 190.2 108.6 22.8 23 B ILE N 729 188.1 108.4 23.6 23 B ILE CA 729 188.5 108.9 25.0 21 B ILE CB 729 187.3 108.9 26.0 21 B ILE CG2 729 187.8 109.2 27.4 20 B ILE CG1 729 186.2 109.8 25.5 19 B ILE CD1 729 184.9 109.7 26.2 19 B ILE C 729 189.6 108.0 25.6 22 B ILE O 729 190.6 108.5 26.1 23 B ALA N 730 189.5 106.7 25.4 22 B ALA CA 730 190.5 105.7 25.9 21 B ALA CB 730 190.1 104.3 25.6 22 B ALA C 730 191.9 106.0 25.3 23 B ALA O 730 192.9 105.6 25.8 22 B ARG N 731 191.9 106.7 24.1 24 B ARG CA 731 193.2 107.0 23.5 24 B ARG CB 731 193.0 107.3 22.0 25 B ARG CG 731 192.7 106.0 21.2 25 B ARG CD 731 193.1 106.1 19.8 25 B ARG NE 731 192.3 107.0 19.0 25 B ARC CZ 731 192.8 108.0 18.3 27 B ARG NH1 731 194.1 108.2 18.2 25 B ARG NH2 731 192.0 108.8 17.6 27 B ARG C 731 193.8 108.3 24.1 24 B ARG O 731 195.0 108.7 23.7 22 B CYS N 732 193.1 109.0 24.9 24 B CYS CA 732 193.5 110.2 25.6 23 B CYS CB 732 192.4 111.0 25.9 22 B CYS SG 732 191.6 111.7 24.4 22 B CYS C 732 194.3 109.8 26.8 23 B CYS O 732 195.1 110.6 27.4 24 B GLN N 733 194.2 108.5 27.2 23 B GLN CA 733 195.0 108.0 28.4 23 B GLN CB 733 194.4 106.8 29.0 23 B GLN CG 733 195.1 106.3 30.3 23 B GLN CD 733 194.5 105.1 31.0 24 B GLN OE1 733 193.9 104.2 30.4 25 B GLN NE2 733 194.6 105.1 32.3 24 B GLN C 733 196.4 107.8 27.9 23 B GLN O 733 196.7 107.1 26.9 24 B ASN N 734 197.4 108.4 28.6 24 B ASN CA 734 198.8 108.3 28.2 23 B ASN CB 734 199.4 109.7 27.9 23 B ASN CG 734 199.8 110.4 29.2 23 B ASN OD1 734 199.3 110.0 30.3 22 B ASN ND2 734 200.5 111.5 29.1 22 B ASN C 734 199.7 107.5 29.2 22 B ASN O 734 199.2 106.9 30.1 23 B TRP N 735 201.0 107.5 28.9 22 B TRP CA 735 202.0 106.8 29.8 23 B TRP CB 735 203.4 107.1 29.3 21 B TRP CG 735 203.7 108.6 29.2 21 B TRP CD2 735 204.4 109.3 30.2 21 B TRP CE2 735 204.5 110.7 29.7 21 B TRP CE3 735 205.0 109.0 31.4 21 B TRP CD1 735 203.4 109.5 28.2 22 B TRP NE1 735 203.8 110.7 28.5 21 B TRP CZ2 735 205.1 111.7 30.5 22 B TRP CZ3 735 205.7 110.0 32.1 21 B TRP CH2 735 205.7 111.3 31.6 21 B TRP C 735 201.9 107.2 31.3 26 B TRP O 735 202.3 106.3 32.1 27 B GLU N 736 201.4 108.3 31.6 26 B GLU CA 736 201.3 108.8 33.0 25 B GLU CB 736 201.0 110.3 33.0 25 B GLU CG 736 202.1 111.2 32.5 25 B GLU CD 736 201.8 112.7 32.5 25 B GLU OE1 736 201.4 113.2 31.4 24 B GLU OE2 736 201.8 113.3 33.6 25 B GLU C 736 200.2 108.1 33.8 25 B GLU O 736 200.3 108.1 35.0 29 B GLY N 737 199.1 107.7 33.1 23 B GLY CA 737 198.0 107.1 33.9 21 B GLY C 737 196.8 108.0 33.8 21 B GLY O 737 195.7 107.6 33.9 22 B GLY N 738 197.1 109.3 33.5 20 B GLY CA 738 196.0 110.3 33.4 19 B GLY C 738 195.5 110.4 32.0 18 B GLY O 738 196.0 109.6 31.1 18 B ILE N 739 194.6 111.3 31.8 17 B ILE CA 739 194.1 111.6 30.5 17 B ILE CB 739 192.5 111.4 30.5 16 B ILE CG2 739 191.9 111.8 29.2 16 B ILE CG1 739 192.2 109.9 30.9 16 B ILE CD1 739 190.8 109.6 31.0 15 B ILE C 739 194.4 113.0 30.0 17 B ILE O 739 194.3 113.9 30.8 18 B GLY N 740 194.8 113.1 28.7 17 B GLY CA 740 195.0 114.4 28.1 15 B GLY C 740 193.9 114.9 27.4 16 B GLY O 740 192.8 114.2 27.2 16 B GLY N 741 194.0 116.1 26.8 17 B GLY CA 741 192.9 116.7 26.0 19 B GLY C 741 192.6 116.0 24.7 19 B GLY O 741 191.4 115.9 24.3 20 B VAL N 742 193.6 115.4 24.1 20 B VAL CA 742 193.5 114.7 22.8 20 B VAL CB 742 193.8 115.6 21.6 19 B VAL CG1 742 192.7 116.6 21.5 18 B VAL CG2 742 195.2 116.2 21.7 19 B VAL C 742 194.6 113.6 22.9 20 B VAL O 742 195.5 113.8 23.7 21 B PRO N 743 194.5 112.6 22.1 20 B PRO CD 743 193.5 112.1 21.2 19 B PRO CA 743 195.6 111.6 22.2 20 B PRO CB 743 195.2 110.6 21.1 19 B PRO CG 743 193.7 110.6 21.2 19 B PRO C 743 197.0 112.1 22.0 21 B PRO O 743 197.2 113.0 21.1 23 B GLY N 744 197.9 111.7 22.9 21 B GLY CA 744 199.3 112.2 22.8 21 B GLY C 744 199.6 113.3 23.8 22 B GLY O 744 200.8 113.5 24.1 22 B MET N 745 198.6 114.0 24.3 21 B MET CA 745 198.9 115.1 25.2 21 B MET CB 745 197.8 116.2 25.1 21 B MET CG 745 198.2 117.2 24.0 19 B MET SD 745 199.8 117.9 24.3 21 B MET CE 745 199.4 119.1 25.4 21 B MET C 745 199.1 114.7 26.7 22 B MET O 745 198.7 113.6 27.1 22 B GLU N 746 199.7 115.6 27.4 22 B GLU CA 746 200.0 115.4 28.8 22 B GLU CB 746 200.8 116.7 29.3 22 B GLU CG 746 201.2 116.6 30.7 25 B GLU CD 746 201.8 117.9 31.2 26 B GLU OE1 746 201.6 118.9 30.5 27 B GLU OE2 746 202.4 117.9 32.3 27 B GLU C 746 198.8 115.2 29.6 22 B GLU O 746 197.7 115.9 29.4 24 B ALA N 747 198.8 114.4 30.6 22 B ALA CA 747 197.7 114.1 31.5 22 B ALA CB 747 198.0 112.9 32.4 21 B ALA C 747 197.3 115.3 32.3 21 B ALA O 747 198.2 115.9 33.0 23 B HIS N 748 196.0 115.7 32.4 21 B HIS CA 748 195.5 116.9 33.1 20 B HIS CB 748 195.3 118.0 32.2 17 B HIS CG 748 195.3 119.4 32.8 15 B HIS CD2 748 196.3 120.3 33.0 14 B HIS ND1 748 194.2 119.9 33.4 15 B HIS CE1 748 194.5 121.1 34.0 14 B HIS NE2 748 195.8 121.3 33.7 14 B HIS C 748 194.3 116.5 33.9 21 B HIS O 748 193.5 115.7 33.5 22 B GLY N 749 194.1 117.1 35.1 22 B GLY CA 749 192.9 116.9 35.9 20 B GLY C 749 191.6 117.3 35.2 20 B GLY O 749 190.6 116.6 35.3 23 B GLY N 750 191.5 118.4 34.6 20 B GLY CA 750 190.3 118.9 34.0 18 B GLY C 750 189.9 117.9 32.9 19 B GLY O 750 188.7 117.6 32.7 20 B TYR N 751 190.8 117.4 32.1 18 B TYR CA 751 190.6 116.5 31.0 17 B TYR CB 751 191.7 116.5 30.0 14 B TYR CG 751 191.8 117.7 29.2 12 B TYR CD1 751 193.0 118.4 29.0 12 B TYR CE1 751 193.1 119.6 28.3 13 B TYR CD2 751 190.7 118.3 28.6 12 B TYR CE2 751 190.7 119.5 27.9 12 B TYR CZ 751 191.9 120.1 27.8 13 B TYR OH 751 192.0 121.3 27.1 15 B TYR C 751 190.3 115.1 31.5 18 B TYR O 751 189.5 114.4 31.0 18 B THR N 752 191.1 114.7 32.6 18 B THR CA 752 190.9 113.4 33.2 19 B THR CB 752 191.9 113.1 34.2 19 B THR OG1 752 193.2 113.3 33.6 18 B THR CG2 752 191.8 111.6 34.7 19 B THR C 752 189.5 113.2 33.8 21 B THR O 752 188.9 112.1 33.8 22 B PHE N 753 188.9 114.3 34.3 21 B PHE CA 753 187.6 114.2 34.9 20 B PHE CB 753 187.3 115.5 35.7 18 B PHE CG 753 185.9 115.5 36.2 18 B PHE CD1 753 185.5 114.7 37.3 17 B PHE CD2 753 184.9 116.1 35.5 17 B PHE CE1 753 184.1 114.6 37.6 17 B PHE CE2 753 183.6 116.0 35.8 18 B PHE CZ 753 183.2 115.2 36.9 18 B PHE C 753 186.6 114.1 33.7 21 B PHE O 753 185.7 113.3 33.8 22 B CYS N 754 186.8 114.9 32.7 22 B CYS CA 754 185.9 114.8 31.5 23 B CYS CB 754 186.3 115.8 30.4 22 B CYS SG 754 186.0 117.5 30.9 21 B CYS C 754 186.0 113.4 30.9 23 B CYS O 754 184.9 112.8 30.6 22 B GLY N 755 187.2 112.8 30.8 23 B GLY CA 755 187.4 111.5 30.3 24 B GLY C 755 186.7 110.4 31.1 26 B GLY O 755 185.8 109.7 30.5 26 B LEU N 756 187.1 110.3 32.3 26 B LEU CA 756 186.5 109.3 33.2 26 B LEU CB 756 187.2 109.2 34.5 25 B LEU CG 756 186.7 108.1 35.5 25 B LEU CD1 756 186.8 106.7 34.8 25 B LEU CD2 756 187.5 108.1 36.7 24 B LEU C 756 185.0 109.4 33.4 27 B LEU O 756 184.2 108.5 33.1 28 B ALA N 757 184.5 110.6 33.7 27 B ALA CA 757 183.1 110.8 33.9 25 B ALA CB 757 182.8 112.3 34.4 24 B ALA C 757 182.3 110.5 32.6 25 B ALA O 757 181.1 110.0 32.7 25 B ALA N 758 182.8 110.8 31.5 26 B ALA CA 758 182.2 110.5 30.2 26 B ALA CB 758 182.9 111.1 29.1 25 B ALA C 758 182.0 109.0 30.0 26 B ALA O 758 181.0 108.5 29.6 27 B LEU N 759 183.1 108.3 30.4 27 B LEU CA 759 183.1 106.8 30.3 27 B LEU CB 759 184.5 106.2 30.5 25 B LEU CG 759 185.4 106.5 29.3 25 B LEU CD1 759 186.8 105.9 29.5 24 B LEU CD2 759 184.8 105.9 28.0 24 B LEU C 759 182.0 106.2 31.3 28 B LEU O 759 181.3 105.3 30.9 28 B VAL N 760 181.9 106.8 32.4 28 B VAL CA 760 181.0 106.3 33.4 27 B VAL CB 760 181.1 107.1 34.7 27 B VAL CG1 760 180.0 106.9 35.7 27 B VAL CG2 760 182.4 106.7 35.5 27 B VAL C 760 179.6 106.5 32.9 28 B VAL O 760 178.8 105.6 33.0 30 B ILE N 761 179.3 107.6 32.2 28 B ILE CA 761 178.0 107.8 31.7 28 B ILE CB 761 177.9 109.3 31.1 27 B ILE CG2 761 176.5 109.4 30.5 27 B ILE CG1 761 178.1 110.3 32.1 27 B ILE CD1 761 178.0 111.8 31.7 27 B ILE C 761 177.8 106.8 30.6 29 B ILE O 761 176.7 106.3 30.4 29 B LEU N 762 178.8 106.5 29.8 31 B LEU CA 762 178.7 105.5 28.7 32 B LEU CB 762 179.8 105.8 27.7 30 B LEU CG 762 179.6 107.1 26.9 29 B LEU CD1 762 180.7 107.2 25.9 29 B LEU CD2 762 178.3 107.2 26.3 28 B LEU C 762 178.9 104.1 29.2 33 B LEU O 762 178.7 103.1 28.5 33 B LYS N 763 179.1 103.9 30.5 35 B LYS CA 763 179.3 102.6 31.2 37 B LYS CB 763 178.0 101.8 31.0 39 B LYS CG 763 176.8 102.4 31.5 43 B LYS CD 763 175.6 102.0 30.7 46 B LYS CE 763 174.2 102.4 31.2 47 B LYS NZ 763 173.1 101.9 30.4 48 B LYS C 763 180.5 101.9 30.5 37 B LYS O 763 180.4 100.7 30.4 38 B LYS N 764 181.5 102.6 30.2 36 B LYS CA 764 182.7 102.1 29.6 37 B LYS CB 764 182.9 102.7 28.2 37 B LYS CG 764 181.9 102.4 27.2 38 B LYS CD 764 181.7 100.9 27.0 39 B LYS CE 764 180.7 100.7 25.9 41 B LYS NZ 764 179.7 101.7 26.0 43 B LYS C 764 184.0 102.3 30.3 37 B LYS O 764 185.1 102.2 29.7 37 B GLU N 765 183.9 102.7 31.6 39 B GLU CA 765 185.2 102.9 32.4 41 B GLU CB 765 184.9 103.1 33.9 41 B GLU CG 765 183.6 103.7 34.2 42 B GLU CD 765 182.6 102.6 34.4 42 B GLU OE1 765 182.7 101.8 35.4 44 B GLU OE2 765 181.7 102.5 33.5 42 B GLU C 765 186.2 101.9 32.2 42 B GLU O 765 187.4 102.2 32.3 42 B ARG N 766 185.8 100.6 32.0 43 B ARG CA 766 186.7 99.5 31.8 45 B ARG CB 766 185.9 98.2 31.6 48 B ARG CG 766 185.5 97.5 32.9 53 B ARG CD 766 184.1 98.0 33.4 57 B ARG NE 766 184.1 98.3 34.8 60 B ARG CZ 766 183.0 98.8 35.4 61 B ARG NH1 766 183.1 99.0 36.7 62 B ARG NH2 766 181.9 99.1 34.8 61 B ARG C 766 187.6 99.7 30.6 43 B ARG O 766 188.6 99.0 30.5 43 B SER N 767 187.3 100.7 29.7 42 B SER CA 767 188.2 101.0 28.5 42 B SER CB 767 187.4 101.9 27.6 42 B SER OG 767 186.1 101.4 27.3 44 B SER C 767 189.5 101.6 28.9 41 B SER O 767 190.3 102.0 28.0 41 B LEU N 768 189.7 101.9 30.2 39 B LEU CA 768 190.9 102.6 30.7 38 B LEU CB 768 190.5 103.9 31.4 38 B LEU CG 768 189.7 105.0 30.8 39 B LEU CD1 768 189.3 106.0 31.8 39 B LEU CD2 768 190.5 105.7 29.7 38 B LEU C 768 191.6 101.7 31.6 38 B LEU O 768 191.1 100.8 32.2 39 B ASN N 769 192.9 102.0 31.8 35 B ASN CA 769 193.7 101.2 32.8 34 B ASN CB 769 195.2 101.3 32.5 34 B ASN CG 769 196.0 100.6 33.5 36 B ASN OD1 769 195.5 100.4 34.6 36 B ASN ND2 769 197.2 100.2 33.1 37 B ASN C 769 193.4 102.0 34.1 34 B ASN O 769 194.0 103.0 34.4 34 B LEU N 770 192.4 101.5 34.8 33 B LEU CA 770 191.9 102.1 36.0 32 B LEU CB 770 190.6 101.5 36.5 30 B LEU CG 770 189.4 101.6 35.6 29 B LEU CD1 770 188.2 101.0 36.2 29 B LEU CD2 770 189.2 103.1 35.1 29 B LEU C 770 193.0 102.1 37.1 33 B LEU O 770 193.0 102.9 38.1 34 B LYS N 771 194.0 101.2 37.0 35 B LYS CA 771 195.0 101.1 38.0 37 B LYS CB 771 195.7 99.8 38.1 40 B LYS CG 771 195.0 98.8 39.0 45 B LYS CD 771 194.7 99.4 40.4 48 B LYS CE 771 193.8 98.4 41.2 50 B LYS NZ 771 192.4 98.2 40.8 51 B LYS C 771 196.0 102.3 37.9 36 B LYS O 771 196.3 103.0 38.9 36 B SER N 772 196.5 102.5 36.7 35 B SER CA 772 197.5 103.5 36.4 35 B SER CB 772 196.0 103.4 35.0 35 B SER OG 772 197.0 103.4 34.0 36 B SER C 772 196.8 104.8 36.6 34 B SER O 772 197.4 105.8 37.0 35 B LEU N 773 195.5 104.9 36.3 33 B LEU CA 773 194.7 106.1 36.4 34 B LEU CB 773 193.4 105.9 35.7 33 B LEU CG 773 192.3 107.0 36.0 33 B LEU CD1 773 192.8 108.4 36.0 34 B LEU CD2 773 191.1 106.8 35.0 33 B LEU C 773 194.6 106.4 37.9 35 B LEU O 773 194.9 107.5 38.3 36 B LEU N 774 194.3 105.3 38.7 36 B LEU CA 774 194.1 105.5 40.1 35 B LEU CB 774 193.8 104.2 40.8 35 B LEU CG 774 193.8 104.2 42.3 34 B LEU CD1 774 192.7 105.2 42.8 33 B LEU CD2 774 193.5 102.8 42.9 34 B LEU C 774 195.4 106.0 40.7 34 B LEU O 774 195.4 107.0 41.5 35 B GLN N 775 196.5 105.5 40.3 35 B GLN CA 775 197.8 105.8 40.8 35 B GLN CB 775 198.9 104.9 40.3 37 B GLN CG 775 200.3 105.2 40.7 43 B GLN CD 775 201.3 104.1 40.3 47 B GLN OE1 775 202.2 103.8 41.1 49 B GLN NE2 775 201.0 103.5 39.1 48 B GLN C 775 198.2 107.3 40.5 35 B GLN O 775 198.8 108.0 41.3 35 B TRP N 776 197.9 107.7 39.3 33 B TRP CA 776 198.2 109.1 38.8 30 B TRP CB 776 198.0 109.2 37.3 27 B TRP CG 776 198.2 110.6 36.8 24 B TRP CD2 776 197.1 111.5 36.5 23 B TRP CE2 776 197.7 112.7 36.0 22 B TRP CE3 776 195.7 111.5 36.8 24 B TRP CD1 776 199.3 111.1 36.4 23 B TRP NE1 776 199.1 112.4 35.9 23 B TRP CZ2 776 197.0 113.8 35.7 24 B TRP CZ3 776 195.0 112.6 36.4 24 B TRP CH2 776 195.6 113.8 35.9 24 B TRP C 776 197.3 110.2 39.6 29 B TRP O 776 197.9 111.1 40.1 29 B VAL N 777 196.0 110.0 39.7 29 B VAL CA 777 195.2 110.9 40.4 28 B VAL CB 777 193.7 110.6 40.3 27 B VAL CG1 777 193.4 109.3 40.9 26 B VAL CG2 777 192.8 111.6 40.9 27 B VAL C 777 195.6 111.1 41.8 30 B VAL O 777 195.7 112.3 42.3 30 B THR N 778 195.9 110.0 42.5 30 B THR CA 778 196.3 110.1 43.9 29 B THR CB 778 196.4 108.7 44.6 28 B THR OG1 778 197.3 107.9 43.9 28 B THR CG2 778 195.0 108.0 44.5 28 B THR C 778 197.6 110.8 44.1 30 B THR O 778 197.9 111.6 45.0 32 B SER N 779 198.5 110.6 43.1 29 B SER CA 779 199.8 111.3 43.1 28 B SER CB 779 200.7 110.7 41.9 28 B SER OG 779 201.0 109.4 42.1 30 B SER C 779 199.7 112.8 42.9 28 B SER O 779 200.6 113.5 43.1 29 B ARG N 780 198.5 113.3 42.5 27 B ARG CA 780 198.3 114.7 42.3 27 B ARG CB 780 197.2 114.9 41.2 26 B ARG CG 780 197.4 114.2 39.9 25 B ARG CD 780 198.3 114.9 38.9 22 B ARG NE 780 199.7 115.0 39.4 21 B ARG CZ 780 200.5 114.0 39.4 21 B ARG NH1 780 200.1 112.8 39.0 22 B ARG NH2 780 201.8 114.1 39.9 22 B ARG C 780 198.0 115.5 43.5 29 B ARG O 780 198.0 116.7 43.4 30 B GLN N 781 197.7 114.8 44.6 31 B GLN CA 781 197.4 115.6 45.8 32 B GLN CB 781 196.7 114.7 46.9 33 B GLN CG 781 196.1 115.6 48.0 33 B GLN CD 781 195.1 114.8 48.9 34 B GLN OE1 781 195.0 113.6 48.9 35 B GLN NE2 781 194.2 115.6 49.5 33 B GLN C 781 198.8 116.0 46.4 32 B GLN O 781 199.7 115.2 46.4 32 B MET N 782 198.8 117.3 46.7 32 B MET CA 782 200.1 117.9 47.2 32 B MET CB 782 200.1 119.4 47.0 31 B MET CG 782 199.8 119.9 45.6 31 B MET SD 782 200.9 119.1 44.4 30 B MET CE 782 202.4 120.0 44.6 29 B MET C 782 200.3 117.6 48.7 33 B MET O 782 199.4 118.0 49.6 33 B ARG N 783 201.3 116.8 49.0 35 B ARG CA 783 201.7 116.4 50.4 37 B ARG CB 783 203.0 115.6 50.4 37 B ARG CG 783 204.1 116.4 49.9 40 B ARG CD 783 205.2 115.6 49.2 42 B ARG NE 783 205.6 114.5 50.1 45 B ARG CZ 783 205.9 113.3 49.7 47 B ARG NH1 783 206.0 113.0 48.4 47 B ARG NH2 783 206.3 112.4 50.6 47 B ARG C 783 201.8 117.5 51.4 37 B ARG O 783 201.4 117.4 52.6 39 B PHE N 784 202.2 118.7 51.0 37 B PHE CA 784 202.3 119.8 51.8 35 B PHE CB 784 203.6 120.7 51.5 36 B PHE CG 784 203.8 121.8 52.5 36 B PHE CD1 784 204.6 121.5 53.6 36 B PHE CD2 784 203.2 123.0 52.4 37 B PHE CE1 784 204.8 122.5 54.6 37 B PHE CE2 784 203.3 123.9 53.4 37 B PHE CZ 784 204.1 123.7 54.5 37 B PHE C 784 201.1 120.7 51.9 34 B PHE O 784 200.5 120.9 52.9 36 B GLU N 785 200.7 121.2 50.7 32 B GLU CA 785 199.5 122.0 50.6 30 B GLU CB 785 199.4 122.8 49.3 30 B GLU CG 785 200.7 123.6 49.0 32 B GLU CD 785 201.7 122.7 48.2 33 B GLU OE1 785 201.6 122.6 47.0 35 B GLU OE2 785 202.6 122.1 48.8 34 B GLU C 785 198.2 121.3 50.9 30 B GLU O 785 197.2 121.9 51.3 29 B GLY N 786 198.2 120.0 50.6 29 B GLY CA 786 197.0 119.2 50.7 29 B GLY C 786 195.9 119.3 49.6 30 B GLY O 786 195.0 118.5 49.5 29 B GLY N 787 196.0 120.4 48.8 29 B GLY CA 787 195.1 120.6 47.7 29 B GLY C 787 195.7 119.8 46.5 28 B GLY O 787 196.8 119.2 46.6 28 B PHE N 788 195.0 119.8 45.4 28 B PHE CA 788 195.4 119.0 44.2 26 B PHE CB 788 194.3 118.3 43.6 25 B PHE CG 788 194.0 116.9 44.3 26 B PHE CD1 788 193.0 116.9 45.3 26 B PHE CD2 788 194.5 115.8 43.9 26 B PHE CE1 788 192.7 115.7 45.9 25 B PHE CE2 788 194.2 114.5 44.5 25 B PHE CZ 788 193.3 114.5 45.5 25 B PHE C 788 196.1 119.9 43.1 25 B PHE O 788 195.7 121.1 43.0 25 B GLN N 789 197.0 119.3 42.4 25 B GLN CA 789 197.7 120.0 41.3 25 B GLN CB 789 199.2 119.7 41.2 24 B GLN CG 789 199.5 118.2 40.9 24 B GLN CD 789 201.0 117.9 41.0 24 B GLN OE1 789 201.4 116.8 40.8 25 B GLN NE2 789 201.8 118.9 41.2 26 B GLN C 789 197.0 119.5 40.0 24 B GLN O 789 196.5 118.4 39.9 25 B GLY N 790 197.1 120.4 38.9 24 B GLY CA 790 196.4 120.0 37.7 22 B GLY C 790 197.1 118.9 36.9 21 B GLY O 790 196.5 118.1 36.3 21 B ARG N 791 198.5 118.9 37.0 21 B ARG CA 791 199.2 118.0 36.3 22 B ARG CB 791 199.4 118.3 34.8 21 B ARG CG 791 199.5 119.8 34.5 21 B ARG CD 791 199.6 120.2 33.0 20 B ARG NE 791 199.5 121.7 32.9 19 B ARG CZ 791 200.0 122.3 31.8 19 B ARG NH1 791 200.7 121.7 30.9 19 B ARG NH2 791 199.9 123.7 31.8 18 B ARG C 791 200.6 117.9 37.0 23 B ARG O 791 201.0 118.8 37.7 24 B CYS N 792 201.3 116.8 36.9 23 B CYS CA 792 202.5 116.6 37.5 24 B CYS CB 792 203.2 115.3 37.0 22 B CYS SG 792 204.7 114.9 37.8 25 B CYS C 792 203.5 117.7 37.4 25 B CYS O 792 203.7 118.3 36.3 27 B ASN N 793 204.1 118.1 38.5 26 B ASN CA 793 205.1 119.2 38.5 27 B ASN CB 793 206.3 118.8 37.7 27 B ASN CG 793 207.5 118.2 38.5 27 B ASN OD1 793 207.7 118.6 39.6 28 B ASN ND2 793 208.2 117.3 37.9 26 B ASN C 793 204.6 120.6 38.2 26 B ASN O 793 205.3 121.4 37.7 26 B LYS N 794 203.3 120.7 38.5 26 B LYS CA 794 202.6 122.0 38.3 25 B LYS CB 794 201.4 121.8 37.4 25 B LYS CG 794 201.2 122.8 36.4 26 B LYS CD 794 202.3 122.9 35.4 25 B LYS CE 794 201.9 123.9 34.3 24 B LYS NZ 794 201.5 125.2 34.8 22 B LYS C 794 202.2 122.5 39.7 26 B LYS O 794 202.6 121.9 40.7 25 B LEU N 795 201.4 123.5 39.8 26 B LEU CA 795 201.0 124.1 41.1 25 B LEU CB 795 201.2 125.6 41.2 23 B LEU CG 795 202.6 126.2 40.8 22 B LEU CD1 795 202.5 127.7 40.9 21 B LEU CD2 795 203.6 125.6 41.7 21 B LEU C 795 199.6 123.7 41.6 25 B LEU O 795 198.8 123.5 40.8 26 B VAL N 796 199.4 123.8 42.9 26 B VAL CA 796 198.1 123.5 43.5 26 B VAL CB 796 198.0 123.7 45.0 27 B VAL CG1 796 197.4 122.5 45.7 28 B VAL CG2 796 199.3 124.2 45.5 28 B VAL C 796 197.1 124.6 43.0 25 B VAL O 796 197.5 125.7 42.6 27 B ASP N 797 195.8 124.2 43.0 24 B ASP CA 797 194.8 125.2 42.6 23 B ASP CB 797 194.7 125.3 41.0 21 B ASP CG 797 193.6 126.1 40.5 20 B ASP OD1 797 192.6 126.5 41.2 22 B ASP OD2 797 193.6 126.4 39.3 20 B ASP C 797 193.5 124.6 43.1 23 B ASP O 797 193.1 123.5 42.9 25 B GLY N 798 192.8 125.5 43.8 24 B GLY CA 798 191.5 125.1 44.4 24 B GLY C 798 190.5 124.4 43.6 25 B GLY O 798 189.7 123.5 44.1 26 B CYS N 799 190.4 124.7 42.3 25 B CYS CA 799 189.3 124.1 41.4 24 B CYS CB 799 189.2 124.8 40.1 25 B CYS SG 799 190.6 124.9 39.0 26 B CYS C 799 189.6 122.7 41.2 24 B CYS O 799 188.7 121.9 40.9 24 B TYR N 800 190.9 122.2 41.4 24 B TYR CA 800 191.2 120.8 41.2 27 B TYR CB 800 192.7 120.6 40.9 26 B TYR CG 800 193.2 121.3 39.6 27 B TYR CD1 800 194.3 122.1 39.7 27 B TYR CE1 800 194.7 122.7 38.5 28 B TYR CD2 800 192.5 121.1 38.4 27 B TYR CE2 800 192.9 121.7 37.3 28 B TYR CZ 800 194.0 122.6 37.3 29 B TYR OH 800 194.4 123.2 36.2 29 B TYR C 800 190.7 120.0 42.4 29 B TYR O 800 190.9 118.8 42.4 30 B SER N 801 190.2 120.7 43.4 30 B SER CA 801 189.7 119.9 44.6 30 B SER CB 801 189.2 121.0 45.6 31 B SER OG 801 190.2 121.8 46.0 31 B SER C 801 188.5 119.1 44.0 29 B SER O 801 188.2 118.1 44.6 30 B PHE N 802 187.9 119.6 42.9 29 B PHE CA 802 186.8 118.9 42.3 28 B PHE CB 802 185.7 119.7 41.8 28 B PHE CG 802 184.6 118.9 41.1 29 B PHE CD1 802 183.6 118.2 41.9 28 B PHE CD2 802 184.6 118.8 39.7 29 B PHE CE1 802 182.7 117.4 41.2 29 B PHE CE2 802 183.7 118.0 39.1 29 B PHE CZ 802 182.7 117.3 39.8 29 B PHE C 802 187.3 118.0 41.1 28 B PHE O 802 187.0 116.8 41.0 30 B TRP N 803 187.9 118.7 40.1 26 B TRP CA 803 188.4 118.0 38.9 24 B TRP CB 803 189.2 119.0 38.0 20 B TRP CG 803 188.4 120.2 37.6 17 B TRP CD2 803 187.1 120.2 36.9 17 B TRP CE2 803 186.8 121.5 36.6 16 B TRP CE3 803 186.2 119.2 36.4 18 B TRP CD1 803 188.8 121.4 37.7 16 B TRP NE1 803 187.8 122.3 37.1 17 B TRP CZ2 803 185.7 121.9 35.9 17 B TRP CZ3 803 185.1 119.6 35.8 18 B TRP CH2 803 184.8 121.0 35.5 18 B TRP C 803 189.2 116.8 39.1 24 B TRP O 803 189.1 115.8 38.4 26 B GLN N 804 190.1 116.9 40.1 26 B GLN CA 804 191.0 115.8 40.5 26 B GLN CB 804 192.3 116.3 41.0 25 B GLN CG 804 193.1 117.0 39.9 25 B GLN CD 804 193.9 116.1 39.0 26 B GLN OE1 804 193.3 115.0 38.6 26 B GLN NE2 804 195.1 116.4 38.6 25 B GLN C 804 190.3 114.9 41.6 27 B GLN O 804 190.1 113.7 41.4 29 B ALA N 805 190.0 115.5 42.8 28 B ALA CA 805 189.5 114.7 43.9 28 B ALA CB 805 189.3 115.5 45.1 28 B ALA C 805 188.1 114.1 43.5 28 B ALA O 805 187.8 113.0 44.0 30 B GLY N 806 187.4 114.7 42.5 29 B GLY CA 806 186.2 114.2 42.1 29 B GLY C 806 186.3 112.8 41.4 31 B GLY O 806 185.4 112.1 41.3 31 B LEU N 807 187.6 112.6 40.9 31 B LEU CA 807 187.9 111.3 40.3 33 B LEU CB 807 189.3 111.3 39.6 33 B LEU CG 807 189.5 112.1 38.3 33 B LEU CD1 807 191.0 112.3 38.1 33 B LEU CD2 807 188.9 111.3 37.2 33 B LEU C 807 187.8 110.1 41.2 33 B LEU O 807 187.4 109.0 40.7 33 B LEU N 808 188.1 110.2 42.5 33 B LEU CA 808 188.0 109.2 43.4 32 B LEU CB 808 188.8 109.6 44.7 31 B LEU CG 808 190.2 109.6 44.1 32 B LEU CD1 808 191.1 110.7 44.7 32 B LEU CD2 808 190.9 108.3 44.2 31 B LEU C 808 186.6 108.6 43.6 32 B LEU O 808 186.5 107.3 43.8 33 B PRO N 809 185.6 109.4 43.7 31 B PRO CD 809 185.5 110.8 44.0 31 B PRO CA 809 184.3 108.8 43.9 31 B PRO CB 809 183.3 110.0 44.0 31 B PRO CG 809 184.2 111.0 44.6 31 B PRO C 809 184.0 107.9 42.7 33 B PRO O 809 183.6 106.8 42.8 33 B LEU N 810 184.3 108.5 41.5 33 B LEU CA 810 184.1 107.8 40.2 32 B LEU CB 810 184.5 108.7 39.1 30 B LEU CG 810 183.7 109.9 38.9 29 B LEU CD1 810 184.1 110.7 37.7 30 B LEU CD2 810 182.2 109.5 38.7 29 B LEU C 810 184.8 106.5 40.1 33 B LEU O 810 184.3 105.5 39.7 34 B LEU N 811 186.1 106.5 40.6 35 B LEU CA 811 186.9 105.3 40.6 37 B LEU CB 811 188.4 105.6 40.8 34 B LEU CG 811 189.2 106.1 39.6 32 B LEU CD1 811 190.5 106.6 40.1 30 B LEU CD2 811 189.3 105.0 38.6 30 B LEU C 811 186.4 104.2 41.6 41 B LEU O 811 186.7 103.1 41.5 42 B HIS N 812 185.7 104.7 42.6 44 B HIS CA 812 185.1 103.8 43.6 46 B HIS CB 812 184.6 104.5 44.8 48 B HIS CG 812 184.8 103.9 46.1 50 B HIS CD2 812 184.2 102.9 46.8 50 B HIS ND1 812 186.0 104.1 46.8 51 B HIS CE1 812 186.0 103.3 47.9 51 B HIS NE2 812 184.9 102.6 47.9 51 B HIS C 812 184.1 103.0 42.9 47 B HIS O 812 184.1 101.7 43.0 47 B ARG N 813 183.1 103.6 42.3 48 B ARG CA 813 182.0 103.0 41.5 49 B ARG CB 813 181.3 104.0 40.6 52 B ARG CG 813 180.3 104.9 41.3 57 B ARG CD 813 179.9 106.1 40.4 60 B ARG NE 813 178.8 106.9 41.0 63 B ARG CZ 813 178.7 107.5 42.1 64 B ARG NH1 813 179.8 107.6 42.9 64 B ARG NH2 813 177.6 108.2 42.5 64 B ARG C 813 182.6 101.9 40.6 48 B ARG O 813 182.4 100.8 40.8 48 B ALA N 814 183.5 102.4 39.7 47 B ALA CA 814 184.1 101.5 38.8 46 B ALA CB 814 185.1 102.3 37.9 45 B ALA C 814 184.8 100.3 39.4 46 B ALA O 814 184.4 99.2 39.1 47 B LEU N 815 185.8 100.5 40.3 47 B LEU CA 815 186.5 99.4 40.9 48 B LEU CB 815 187.6 99.9 41.9 47 B LEU CG 815 188.8 100.6 41.3 48 B LEU CD1 815 189.8 101.1 42.4 47 B LEU CD2 815 189.6 99.6 40.4 48 B LEU C 815 185.6 98.5 41.6 48 B LEU O 815 185.6 97.3 41.5 49 B HIS N 816 184.6 99.1 42.4 49 B HIS CA 816 183.7 98.3 43.1 51 B HIS CB 816 182.9 99.2 44.1 53 B HIS CG 816 181.8 98.5 44.8 55 B HIS CD2 816 181.9 97.6 45.8 56 B HIS ND1 816 180.5 98.7 44.5 56 B HIS CE1 816 179.8 97.9 45.3 57 B HIS NE2 816 180.6 97.2 46.0 57 B HIS C 816 182.7 97.5 42.2 52 B HIS O 816 182.2 96.5 42.7 52 B ALA N 817 182.5 98.0 41.0 52 B ALA CA 817 181.6 97.3 40.1 52 B ALA CB 817 181.2 98.2 39.0 52 B ALA C 817 182.3 96.1 39.6 53 B ALA O 817 181.6 95.2 38.9 53 B GLN N 818 183.6 96.0 39.8 54 B GLN CA 818 184.3 94.8 39.4 55 B GLN CB 818 185.7 95.2 38.8 55 B GLN CG 818 185.5 96.0 37.5 56 B GLN CD 818 186.7 96.8 37.2 57 B GLN OE1 818 187.8 96.5 37.5 57 B GLN NE2 818 186.4 97.9 36.5 57 B GLN C 818 184.5 94.1 40.7 55 B GLN O 818 185.4 93.2 40.9 55 B GLY N 819 183.7 94.4 41.7 56 B GLY CA 819 183.7 93.8 43.0 57 B GLY C 819 185.1 93.9 43.6 57 B GLY O 819 185.6 92.8 44.1 58 B ASP N 820 185.7 95.0 43.6 57 B ASP CA 820 187.1 95.1 44.2 57 B ASP CB 820 187.7 96.5 44.0 56 B ASP CG 820 189.2 96.5 44.1 56 B ASP OD1 820 189.9 96.7 43.0 56 B ASP OD2 820 189.8 96.2 45.2 54 B ASP C 820 186.8 94.9 45.7 57 B ASP O 820 185.8 95.5 46.3 57 B PRO N 821 187.5 94.0 46.3 57 B PRO CD 821 188.3 92.9 45.7 57 B PRO CA 821 187.3 93.7 47.8 58 B PRO CB 821 187.9 92.2 47.9 58 B PRO CG 821 189.0 92.2 46.8 58 B PRO C 821 188.1 94.6 48.7 58 B PRO O 821 187.7 94.9 49.8 60 B ALA N 822 189.3 95.2 48.2 57 B ALA CA 822 190.1 96.1 49.0 55 B ALA CB 822 191.5 96.1 48.3 54 B ALA C 822 189.6 97.5 49.1 55 B ALA O 822 190.2 98.3 49.8 55 B LEU N 823 188.4 97.8 48.6 55 B LEU CA 823 187.8 99.1 48.7 56 B LEU CB 823 186.8 99.3 47.6 55 B LEU CG 823 187.2 99.3 46.2 55 B LEU CD1 823 186.0 99.6 45.3 54 B LEU CD2 823 188.3 100.2 46.0 55 B LEU C 823 187.2 99.5 50.0 57 B LEU O 823 186.2 98.9 50.4 59 B SER N 824 187.7 100.6 50.6 58 B SER CA 824 187.2 101.1 51.9 58 B SER CB 824 188.0 102.3 52.4 58 B SER OG 824 187.5 102.9 53.6 57 B SER C 824 185.7 101.4 51.9 59 B SER O 824 185.2 101.7 50.9 58 B MET N 825 185.1 101.2 53.0 60 B MET CA 825 183.6 101.4 53.1 60 B MET CB 825 182.9 100.2 53.8 63 B MET CG 825 183.1 98.8 53.1 66 B MET SD 825 182.2 98.5 51.5 69 B MET CE 825 183.4 97.4 50.6 68 B MET C 825 183.4 102.7 53.9 59 B MET O 825 182.3 102.8 54.5 59 B SER N 826 184.3 103.6 53.9 58 B SER CA 826 184.2 104.9 54.6 56 B SER CB 826 184.6 104.7 56.1 56 B SER OG 826 186.0 104.4 56.2 56 B SER C 826 184.8 106.1 54.0 55 B SER O 826 184.3 107.2 54.1 54 B HIS N 827 185.9 105.9 53.3 53 B HIS CA 827 186.7 107.0 52.7 50 B HIS CB 827 187.9 107.3 53.6 53 B HIS CG 827 187.7 107.6 55.0 55 B HIS CD2 827 188.1 107.0 56.2 55 B HIS ND1 827 186.9 108.7 55.4 55 B HIS CE1 827 186.8 108.8 56.7 55 B HIS NE2 827 187.6 107.8 57.2 56 B HIS C 827 187.2 106.9 51.3 47 B HIS O 827 187.6 105.8 50.9 45 B TRP N 828 187.2 108.0 50.6 43 B TRP CA 828 187.7 108.0 49.2 39 B TRP CB 828 187.4 109.4 48.6 35 B TRP CG 828 185.9 109.7 48.6 31 B TRP CD2 828 184.9 108.9 48.1 29 B TRP CE2 828 183.7 109.7 48.2 29 B TRP CE3 828 184.8 107.6 47.5 29 B TRP CD1 828 185.4 110.9 49.0 30 B TRP NE1 828 184.0 110.8 48.8 30 B TRP CZ2 828 182.5 109.2 47.8 29 B TRP CZ3 828 183.6 107.2 47.1 29 B TRP CH2 828 182.4 107.9 47.2 29 B TRP C 828 189.1 107.8 49.3 38 B TRP O 828 189.7 108.1 50.4 38 B MET N 829 189.8 107.4 48.2 38 B MET CA 829 191.2 107.2 48.2 38 B MET CB 829 191.5 106.1 47.2 38 B MET CG 829 190.7 104.8 47.4 39 B MET SD 829 191.3 103.4 46.4 39 B MET CE 829 193.1 103.6 46.6 36 B MET C 829 192.1 108.3 48.1 38 B MET O 829 193.1 108.4 47.3 38 B PHE N 830 191.9 109.3 49.0 38 B PHE CA 830 192.7 110.5 49.1 37 B PHE CB 830 192.4 111.6 48.0 33 B PHE CG 830 191.1 112.3 48.1 29 B PHE CD1 830 191.1 113.6 48.7 28 B PHE CD2 830 189.9 111.8 47.6 28 B PHE CE1 830 189.9 114.3 48.8 28 B PHE CE2 830 188.7 112.6 47.7 28 B PHE CZ 830 188.7 113.8 48.3 28 B PHE C 830 192.5 111.1 50.5 38 B PHE O 830 191.5 110.8 51.2 38 B HIS N 831 193.5 112.0 50.9 39 B HIS CA 831 193.3 112.6 52.2 39 B HIS CB 831 194.6 113.2 52.6 39 B HIS CG 831 194.9 113.3 54.1 40 B HIS CD2 831 194.2 113.9 55.1 40 B HIS ND1 831 196.0 112.6 54.6 40 B HIS CE1 831 196.0 112.8 55.9 40 B HIS NE2 831 194.9 113.6 56.2 41 B HIS C 831 192.2 113.6 52.2 39 B HIS O 831 192.4 114.8 51.9 40 B GLN N 832 191.0 113.2 52.6 39 B GLN CA 832 189.8 114.1 52.6 39 B GLN CB 832 188.6 113.4 53.0 39 B GLN CG 832 188.1 112.3 52.0 37 B GLN CD 832 187.1 111.3 52.6 36 B GLN OE1 832 186.1 111.8 53.1 35 B GLN NE2 832 187.3 110.1 52.5 34 B GLN C 832 190.0 115.3 53.6 41 B GLN O 832 189.5 116.4 53.4 40 B GLN N 833 190.7 115.0 54.6 42 B GLN CA 833 191.0 115.9 55.7 43 B GLN CB 833 191.8 115.3 56.9 44 B GLN CG 833 191.5 115.9 58.2 45 B GLN CD 833 192.7 115.8 59.2 45 B GLN OE1 833 193.5 114.8 59.1 45 B GLN NE2 833 192.8 116.7 60.1 45 B GLN C 833 191.9 117.1 55.2 42 B GLN O 833 191.5 118.3 55.3 42 B ALA N 834 193.0 116.8 54.6 41 B ALA CA 834 194.0 117.8 54.0 39 B ALA CB 834 195.2 117.1 53.5 39 B ALA C 834 193.3 118.6 53.0 39 B ALA O 834 193.5 119.8 53.0 40 B LEU N 835 192.6 118.0 52.1 39 B LEU CA 835 191.9 118.8 51.0 39 B LEU CB 835 191.2 117.9 50.0 39 B LEU CG 835 190.4 118.7 49.0 39 B LEU CD1 835 191.3 119.7 48.2 39 B LEU CD2 835 189.7 117.7 48.0 39 B LEU C 835 190.9 119.8 51.7 39 B LEU O 835 190.9 121.0 51.3 41 B GLN N 836 190.2 119.4 52.7 38 B GLN CA 836 189.2 120.2 53.4 39 B GLN CB 836 188.4 119.5 54.4 39 B GLN CG 836 187.2 118.7 53.8 39 B GLN CD 836 186.3 118.1 54.9 39 B GLN OE1 836 185.7 118.8 55.7 38 B GLN NE2 836 186.2 116.8 54.9 39 B GLN C 836 189.9 121.4 54.1 38 B GLN O 836 189.4 122.5 54.2 38 B GLU N 837 191.1 121.1 54.6 38 B GLU CA 837 191.9 122.1 55.3 39 B GLU CB 837 193.0 121.5 56.1 38 B GLU CG 837 192.5 120.7 57.3 39 B GLU CD 837 193.6 120.0 58.1 40 B GLU OE1 837 194.8 120.3 58.0 40 B GLU OE2 837 193.2 119.1 58.9 41 B GLU C 837 192.4 123.1 54.3 39 B GLU O 837 192.0 124.3 54.4 40 B TYR N 838 193.1 122.7 53.3 39 B TYR CA 838 193.6 123.6 52.2 36 B TYR CB 838 194.1 122.8 51.0 37 B TYR CG 838 194.5 123.6 49.8 38 B TYR CD1 838 195.7 124.4 49.9 37 B TYR CE1 838 196.0 125.4 48.9 37 B TYR CD2 838 193.7 123.8 48.7 37 B TYR CE2 838 194.0 124.8 47.7 36 B TYR CZ 838 195.2 125.6 47.9 36 B TYR OH 838 195.4 126.6 47.0 36 B TYR C 838 192.4 124.5 51.8 35 B TYR O 838 192.6 125.7 51.8 35 B ILE N 839 191.3 123.9 51.4 34 B ILE CA 839 190.2 124.7 51.0 33 B ILE CB 839 189.0 123.9 50.5 32 B ILE CG2 839 187.8 124.8 50.1 31 B ILE CG1 839 189.3 123.0 49.3 32 B ILE CD1 839 188.1 122.3 48.7 31 B ILE C 839 189.7 125.7 52.0 34 B ILE O 839 189.4 126.9 51.7 36 B LEU N 840 189.5 125.2 53.3 35 B LEU CA 840 189.1 126.1 54.3 34 B LEU CB 840 188.6 125.3 55.5 33 B LEU CG 840 187.2 124.6 55.2 32 B LEU CD1 840 186.9 123.6 56.3 32 B LEU CD2 840 186.1 125.7 55.2 31 B LEU C 840 190.1 127.2 54.8 35 B LEU O 840 189.7 128.4 55.0 35 B MET N 841 191.3 126.8 54.9 35 B MET CA 841 192.4 127.7 55.3 36 B MET CB 841 193.5 127.0 55.9 37 B MET CG 841 193.2 126.4 57.3 38 B MET SD 841 194.6 125.9 58.2 40 B MET CE 841 194.6 124.2 58.0 38 B MET C 841 192.9 128.6 54.2 36 B MET O 841 193.1 129.8 54.3 37 B CYS N 842 193.3 128.0 53.0 37 B CYS CA 842 193.9 128.7 51.9 36 B CYS CB 842 195.0 127.9 51.3 36 B CYS SG 842 196.1 127.3 52.6 37 B CYS C 842 193.0 129.3 50.8 36 B CYS O 842 193.4 130.4 50.3 37 B CYS N 843 191.9 128.7 50.4 35 B CYS CA 843 191.1 129.2 49.3 36 B CYS CB 843 190.8 128.0 48.4 34 B CYS SG 843 192.3 127.0 48.1 33 B CYS C 843 189.8 129.9 49.5 37 B CYS O 843 188.9 129.9 48.7 38 B GLN N 844 189.7 130.6 50.7 38 B GLN CA 844 188.5 131.4 51.0 39 B GLN CB 844 188.0 130.9 52.3 38 B GLN CG 844 186.5 131.2 52.5 38 B GLN CD 844 185.9 130.2 53.4 38 B GLN OE1 844 184.7 130.0 53.4 38 B GLN NE2 844 186.7 129.5 54.3 38 B GLN C 844 188.8 132.9 51.0 40 B GLN O 844 189.9 133.3 51.5 40 B CYS N 845 187.9 133.7 50.4 40 B CYS CA 845 188.1 135.1 50.4 42 B CYS CB 845 187.7 135.7 49.0 42 B CYS SG 845 187.8 137.5 49.0 43 B CYS C 845 187.2 135.7 51.5 43 B CYS O 845 186.0 135.4 51.6 43 B PRO N 846 187.8 136.5 52.4 44 B PRO CD 846 189.2 137.0 52.4 44 B PRO CA 846 187.1 137.2 53.5 43 B PRO CB 846 188.1 138.2 54.0 44 B PRO CG 846 189.4 137.5 53.8 44 B PRO C 846 185.8 137.9 53.0 43 B PRO O 846 184.8 137.7 53.6 44 B ALA N 847 185.9 138.6 51.9 42 B ALA CA 847 184.8 139.3 51.3 41 B ALA CB 847 185.3 140.4 50.4 41 B ALA C 847 183.7 138.4 50.6 40 B ALA O 847 182.6 138.9 50.2 40 B GLY N 848 184.0 137.1 50.6 39 B GLY CA 848 183.1 136.2 49.9 39 B GLY C 848 183.8 135.7 48.7 39 B GLY O 848 184.7 136.4 48.1 40 B GLY N 849 183.5 134.4 48.3 37 B GLY CA 849 184.2 133.9 47.1 34 B GLY C 849 185.4 133.0 47.5 33 B GLY O 849 186.0 133.1 48.6 32 B LEU N 850 185.6 132.0 46.7 32 B LEU CA 850 186.7 131.0 46.9 31 B LEU CB 850 186.1 129.6 46.8 31 B LEU CG 850 185.3 129.0 48.0 31 B LEU CD1 850 186.1 128.8 49.2 30 B LEU CD2 850 184.0 129.7 48.2 29 B LEU C 850 187.7 131.3 45.8 29 B LEU O 850 187.4 131.9 44.8 28 B LEU N 851 188.9 130.7 45.9 29 B LEU CA 851 189.9 131.0 44.9 31 B LEU CB 851 190.6 132.3 45.3 32 B LEU CG 851 190.9 132.5 46.8 32 B LEU CD1 851 192.3 132.0 47.1 32 B LEU CD2 851 190.8 134.0 47.2 32 B LEU C 851 190.9 129.9 44.6 31 B LEU O 851 190.9 128.8 45.2 33 B ASP N 852 191.8 130.2 43.7 30 B ASP CA 852 192.8 129.3 43.2 29 B ASP CB 852 193.7 130.0 42.2 28 B ASP CG 852 194.9 129.2 41.7 28 B ASP OD1 852 195.4 128.4 42.4 29 B ASP OD2 852 195.3 129.4 40.5 29 B ASP C 852 193.7 128.9 44.5 29 B ASP O 852 193.6 127.8 45.0 29 B LYS N 853 194.5 129.9 44.9 29 B LYS CA 853 195.4 129.7 46.0 28 B LYS CB 853 196.7 129.2 45.6 26 B LYS CG 853 197.5 130.1 44.6 24 B LYS CD 853 198.9 129.6 44.3 23 B LYS CE 853 198.9 128.3 43.5 24 B LYS NZ 853 198.2 128.3 42.2 24 B LYS C 853 195.5 131.1 46.6 30 B LYS O 853 195.0 132.1 46.0 28 B PRO N 854 196.1 131.3 47.8 31 B PRO CD 854 196.6 130.2 48.7 31 B PRO CA 854 196.3 132.6 48.3 32 B PRO CB 854 196.9 132.3 49.7 32 B PRO CG 854 197.6 131.0 49.5 32 B PRO C 854 197.1 133.5 47.4 33 B PRO O 854 198.1 133.2 46.9 33 B GLY N 855 196.6 134.7 47.2 34 B GLY CA 855 197.2 135.7 46.4 36 B GLY C 855 196.4 135.9 45.1 36 B GLY O 855 196.5 136.9 44.5 38 B LYS N 856 195.6 134.9 44.7 35 B LYS CA 856 194.8 134.9 43.5 34 B LYS CB 856 194.6 133.5 43.1 34 B LYS CG 856 195.8 132.8 42.6 34 B LYS CD 856 196.5 133.6 41.6 35 B LYS CE 856 197.9 133.1 41.2 37 B LYS NZ 856 197.8 132.0 40.2 38 B LYS C 856 193.5 135.5 43.9 34 B LYS O 856 193.2 135.6 45.1 34 B SER N 857 192.8 136.1 42.9 34 B SER CA 857 191.5 136.7 43.0 32 B SER CB 857 191.2 137.7 41.9 33 B SER OG 857 191.8 138.9 42.1 36 B SER C 857 190.4 135.7 43.1 32 B SER O 857 190.5 134.6 42.5 32 B ARG N 858 189.3 136.1 43.6 31 B ARG CA 858 188.1 135.3 43.7 31 B ARG CB 858 187.2 135.8 44.9 32 B ARG CG 858 186.5 137.1 44.6 33 B ARG CD 858 186.0 137.8 45.9 34 B ARG NE 858 185.1 138.9 45.6 35 B ARG CZ 858 184.2 139.4 46.5 35 B ARG NH1 858 184.1 138.9 47.7 36 B ARG NH2 858 183.4 140.3 46.1 35 B ARG C 858 187.3 135.4 42.4 30 B ARG O 858 187.4 136.3 41.7 31 B ASP N 859 186.5 134.3 42.2 28 B ASP CA 859 185.6 134.3 41.0 28 B ASP CB 859 186.4 134.1 39.7 28 B ASP CG 859 187.3 132.9 39.7 28 B ASP OD1 859 186.7 131.8 39.5 29 B ASP OD2 859 188.5 133.0 39.7 30 B ASP C 859 184.6 133.1 41.2 27 B ASP O 859 184.9 132.2 42.0 27 B PHE N 860 183.5 133.2 40.5 28 B PHE CA 860 182.5 132.2 40.6 28 B PHE CB 860 181.3 132.7 39.8 28 B PHE CG 860 180.9 134.1 40.2 28 B PHE CD1 860 181.2 135.2 39.5 29 B PHE CD2 860 180.2 134.3 41.4 29 B PHE CE1 860 180.9 136.4 39.9 29 B PHE CE2 860 179.8 135.6 41.8 29 B PHE CZ 860 180.2 136.7 41.1 28 B PHE C 860 182.9 130.8 40.2 28 B PHE O 860 182.5 129.8 40.8 30 B TYR N 861 183.8 130.7 39.2 26 B TYR CA 861 184.4 129.4 38.7 23 B TYR CB 861 185.4 129.6 37.6 20 B TYR CG 861 186.2 128.4 37.3 17 B TYR CD1 861 185.7 127.2 36.9 16 B TYR CE1 861 186.4 126.1 36.7 14 B TYR CD2 861 187.6 128.4 37.5 15 B TYR CE2 861 188.4 127.3 37.3 14 B TYR CZ 861 187.8 126.1 36.9 14 B TYR OH 861 188.5 125.0 36.7 14 B TYR C 861 185.0 128.7 39.9 23 B TYR O 861 184.7 127.5 40.2 23 B HIS N 862 185.9 129.4 40.6 23 B HIS CA 862 186.6 128.8 41.7 25 B HIS CB 862 187.8 129.5 42.1 22 B HIS CG 862 188.9 129.5 41.1 21 B HIS CD2 862 190.0 128.7 41.0 20 B HIS ND1 862 189.0 130.4 40.1 22 B HIS CE1 862 190.1 130.2 39.4 22 B HIS NE2 862 190.8 129.2 40.0 20 B HIS C 862 185.7 128.6 42.9 27 B HIS O 862 185.9 127.7 43.8 28 B THR N 863 184.7 129.5 43.0 28 B THR CA 863 183.7 129.4 44.1 30 B THR CB 863 182.6 130.6 44.1 30 B THR OG1 863 183.3 131.8 44.2 32 B THR CG2 863 181.6 130.4 45.2 30 B THR C 863 183.1 128.1 44.0 30 B THR O 863 183.1 127.2 44.8 32 B CYS N 864 182.6 127.8 42.7 29 B CYS CA 864 181.9 126.6 42.4 28 B CYS CB 864 181.4 126.7 40.9 28 B CYS SG 864 180.7 125.1 40.3 28 B CYS C 864 182.7 125.4 42.6 27 B CYS O 864 182.2 124.4 43.1 29 B TYR N 865 183.9 125.3 42.1 26 B TYR CA 865 184.7 124.1 42.3 26 B TYR CB 865 185.6 123.9 41.0 25 B TYR CG 865 184.8 123.6 39.8 23 B TYR CD1 865 184.5 124.7 38.9 24 B TYR CE1 865 183.6 124.5 37.8 24 B TYR CD2 865 184.3 122.4 39.5 22 B TYR CE2 865 183.4 122.2 38.4 22 B TYR CZ 865 183.1 123.2 37.6 23 B TYR OH 865 182.2 123.0 36.5 23 B TYR C 865 185.4 123.9 43.6 27 B TYR O 865 185.6 122.7 43.9 28 B CYS N 866 185.7 124.9 44.3 29 B CYS CA 866 186.3 124.8 45.7 29 B CYS CB 866 186.7 126.1 46.2 30 B CYS SG 866 188.2 126.7 45.6 32 B CYS C 866 185.2 124.2 46.6 29 B CYS O 866 185.4 123.2 47.3 29 B LEU N 867 183.9 124.7 46.4 28 B LEU CA 867 182.8 124.2 47.2 29 B LEU CB 867 181.6 125.1 47.0 27 B LEU CG 867 181.8 126.5 47.6 27 B LEU CD1 867 180.6 127.4 47.4 27 B LEU CD2 867 182.2 126.4 49.1 27 B LEU C 867 182.5 122.8 46.8 31 B LEU O 867 182.4 121.9 47.6 32 B SER N 868 182.4 122.5 45.5 32 B SER CA 868 182.1 121.2 44.9 31 B SER CB 868 182.2 121.2 43.4 29 B SER OG 868 181.1 122.0 42.8 29 B SER C 868 183.1 120.2 45.5 31 B SER O 868 182.7 119.1 46.0 32 B GLY N 869 184.4 120.5 45.5 32 B GLY CA 869 185.4 119.6 46.0 33 B GLY C 869 185.4 119.4 47.5 35 B GLY O 869 185.9 118.4 48.0 36 B LEU N 870 184.8 120.4 48.2 37 B LEU CA 870 184.7 120.3 49.7 36 B LEU CB 870 184.3 121.6 50.3 35 B LEU CG 870 184.2 121.8 51.8 34 B LEU CD1 870 185.7 121.6 52.3 33 B LEU CD2 870 183.7 123.1 52.2 32 B LEU C 870 183.6 119.3 50.0 36 B LEU O 870 183.9 118.3 50.7 36 B SER N 871 182.5 119.4 49.3 37 B SER CA 871 181.3 118.6 49.5 38 B SER CB 871 180.2 119.0 48.4 38 B SER OG 871 179.1 118.2 48.6 38 B SER C 871 181.8 117.1 49.2 39 B SER O 871 181.4 116.2 49.9 40 B ILE N 872 182.6 116.9 48.1 39 B ILE CA 872 183.1 115.6 47.8 39 B ILE CB 872 183.7 115.6 46.3 37 B ILE CG2 872 184.6 114.4 46.2 35 B ILE CG1 872 182.5 115.5 45.3 37 B ILE CD1 872 183.0 115.5 43.9 38 B ILE C 872 184.0 115.1 48.9 39 B ILE O 872 183.9 113.9 49.3 39 B ALA N 873 184.9 115.9 49.3 40 B ALA CA 873 185.9 115.5 50.3 41 B ALA CB 873 187.0 116.6 50.5 41 B ALA C 873 185.3 115.2 51.7 42 B ALA O 873 185.9 114.5 52.5 42 B GLN N 874 184.1 115.7 51.9 42 B GLN CA 874 183.4 115.4 53.2 43 B GLN CB 874 183.0 116.8 53.8 42 B GLN CG 874 181.8 117.4 53.1 40 B GLN CD 874 181.5 118.8 53.7 39 B GLN OE1 874 180.5 119.4 53.4 40 B GLN NE2 874 182.5 119.3 54.5 37 B GLN C 874 182.3 114.4 53.2 45 B GLN O 874 181.8 114.0 54.2 45 B HIS N 875 181.9 114.0 52.0 46 B HIS CA 875 180.8 113.1 51.9 46 B HIS CB 875 179.6 113.7 51.1 45 B HIS CG 875 178.9 114.8 51.7 45 B HIS CD2 875 178.1 115.8 51.2 45 B HIS ND1 875 179.0 115.0 53.1 45 B HIS CE1 875 178.2 116.1 53.4 45 B HIS NE2 875 177.7 116.6 52.3 44 B HIS C 875 181.2 111.8 51.2 48 B HIS O 875 181.5 111.8 50.0 48 B PHE N 876 181.1 110.7 52.0 51 B PHE CA 876 181.4 109.4 51.4 54 B PHE CB 876 182.5 108.6 52.3 52 B PHE CG 876 182.7 107.2 51.7 51 B PHE CD1 876 183.7 107.0 50.8 51 B PHE CD2 876 181.9 106.2 52.1 51 B PHE CE1 876 183.9 105.7 50.3 51 B PHE CE2 876 182.0 104.9 51.6 51 B PHE CZ 876 183.1 104.7 50.7 52 B PHE C 876 180.1 108.6 51.4 56 B PHE O 876 179.2 108.7 52.2 57 B GLY N 877 180.1 107.7 50.4 60 B GLY CA 877 178.9 106.8 50.2 63 B GLY C 877 179.3 105.6 49.3 64 B GLY O 877 180.1 105.8 48.4 65 B SER N 878 178.8 104.4 49.6 66 B SER CA 878 179.2 103.2 48.8 67 B SER CB 878 180.6 102.7 49.2 66 B SER OG 878 181.1 102.0 48.1 66 B SER C 878 178.1 102.2 49.1 68 B SER O 878 178.3 101.2 49.8 69 B GLY N 879 176.9 102.3 48.4 69 B GLY CA 879 175.9 101.4 48.6 71 B GLY C 879 175.1 101.8 49.9 71 B GLY O 879 174.6 102.9 49.9 72 B ALA N 880 175.2 101.0 50.9 72 B ALA CA 880 174.5 101.3 52.2 72 B ALA CB 880 174.2 100.0 53.0 73 B ALA C 880 175.5 102.2 53.1 72 B ALA O 880 175.0 102.8 54.0 73 B MET N 881 176.7 102.3 52.7 72 B MET CA 881 177.7 103.2 53.3 71 B MET CB 881 179.1 102.9 52.8 72 B MET CG 881 179.8 101.6 53.4 73 B MET SD 881 178.8 100.2 53.2 75 B MET CE 881 178.5 99.9 55.0 75 B MET C 881 177.5 104.6 53.1 70 B MET O 881 177.2 105.1 52.0 69 B LEU N 882 177.7 105.4 54.2 68 B LEU CA 882 177.6 106.9 54.2 66 B LEU CB 882 176.1 107.3 54.3 67 B LEU CG 882 175.2 107.4 53.1 67 B LEU CD1 882 175.9 108.0 52.0 67 B LEU CD2 882 174.6 106.0 52.7 67 B LEU C 882 178.5 107.5 55.3 65 B LEU O 882 178.0 107.6 56.4 66 B HIS N 883 179.7 107.8 55.0 64 B HIS CA 883 180.6 108.4 56.0 61 B HIS CB 883 181.8 107.6 56.2 61 B HIS CG 883 182.7 108.0 57.3 62 B HIS CD2 883 183.3 109.2 57.5 62 B HIS ND1 883 183.1 107.2 58.4 62 B HIS CE1 883 183.9 107.9 59.2 62 B HIS NE2 883 184.0 109.2 58.7 62 B HIS C 883 181.0 109.9 55.7 60 B HIS O 883 181.6 110.1 54.7 60 B ASP N 884 180.6 110.8 56.6 56 B ASP CA 884 181.0 112.2 56.4 53 B ASP CB 884 179.8 113.1 56.8 52 B ASP CG 884 178.6 113.0 55.8 52 B ASP OD1 884 177.8 113.9 55.8 52 B ASP OD2 884 178.6 112.0 55.0 53 B ASP C 884 182.1 112.5 57.3 52 B ASP O 884 182.3 111.9 58.3 52 B VAL N 885 182.9 113.5 56.8 50 B VAL CA 885 184.1 114.0 57.6 49 B VAL CB 885 185.5 113.5 57.0 48 B VAL CG1 885 186.6 114.2 57.7 47 B VAL CG2 885 185.6 112.0 57.1 47 B VAL C 885 183.9 115.5 57.4 49 B VAL O 885 184.0 115.9 56.2 50 B VAL N 886 183.6 116.2 58.4 48 B VAL CA 886 183.4 117.6 58.2 49 B VAL CB 886 182.0 118.1 58.7 48 B VAL CG1 886 181.9 119.6 58.5 48 B VAL CG2 886 181.0 117.3 57.9 48 B VAL C 886 184.5 118.3 59.1 50 B VAL O 886 184.6 117.9 60.3 51 B MET N 887 185.3 119.2 58.5 51 B MET CA 887 186.3 119.9 59.2 51 B MET CB 887 187.5 120.1 58.3 50 B MET CG 887 188.2 118.8 57.9 50 B MET SD 887 188.6 117.8 59.3 49 B MET CE 887 190.1 118.7 59.8 49 B MET C 887 185.9 121.2 59.8 52 B MET O 887 185.1 121.9 59.2 52 B GLY N 888 186.4 121.5 61.0 52 B GLY CA 888 186.1 122.7 61.7 53 B GLY C 888 184.6 122.8 62.2 53 B GLY O 888 184.0 121.7 62.5 53 B VAL N 889 184.0 123.9 62.2 54 B VAL CA 889 182.7 124.0 62.7 56 B VAL CB 889 182.3 125.5 62.7 56 B VAL CG1 889 181.9 126.0 61.4 56 B VAL CG2 889 181.1 125.7 63.7 56 B VAL C 889 181.8 123.2 61.9 57 B VAL O 889 181.8 123.2 60.6 58 B PRO N 890 180.9 122.3 62.5 58 B PRO CD 890 180.7 122.2 63.9 58 B PRO CA 890 180.0 121.4 61.8 58 B PRO CB 890 179.3 120.7 62.9 58 B PRO CG 890 179.3 121.7 64.0 58 B PRO C 890 179.0 122.1 60.8 57 B PRO O 890 178.4 121.4 60.0 57 B GLU N 891 178.9 123.4 61.0 57 B GLU CA 891 178.0 124.2 60.1 58 B GLU CB 891 177.8 125.6 60.6 59 B GLU CG 891 176.8 125.8 61.8 61 B GLU CD 891 177.2 125.0 63.0 63 B GLU OE1 891 178.4 124.8 63.3 63 B GLU OE2 891 176.2 124.7 63.8 64 B GLU C 891 178.6 124.2 58.7 57 B GLU O 891 178.0 124.6 57.7 57 B ASN N 892 179.9 123.7 58.6 54 B ASN CA 892 180.6 123.7 57.4 52 B ASN CB 892 182.1 123.5 57.7 49 B ASN CG 892 182.8 124.7 58.4 47 B ASN OD1 892 183.9 124.5 58.9 45 B ASN ND2 892 182.1 125.8 58.4 45 B ASN C 892 180.2 122.6 56.4 51 B ASN O 892 180.7 122.5 55.3 53 B VAL N 893 179.2 121.8 56.8 49 B VAL CA 893 178.8 120.7 55.9 48 B VAL CB 893 178.1 119.5 56.6 49 B VAL CG1 893 176.7 119.8 57.0 49 B VAL CG2 893 178.2 118.3 55.7 49 B VAL C 893 177.9 121.3 54.8 47 B VAL O 893 176.9 122.0 55.0 47 B LEU N 894 178.2 120.8 53.5 46 B LEU CA 894 177.5 121.3 52.3 44 B LEU CB 894 178.6 121.6 51.2 43 B LEU CG 894 179.6 122.6 51.6 42 B LEU CD1 894 180.8 122.6 50.6 41 B LEU CD2 894 179.0 124.0 51.6 42 B LEU C 894 176.6 120.2 51.8 43 B LEU O 894 176.8 119.0 52.2 42 B GLN N 895 175.6 120.6 51.0 41 B GLN CA 895 174.7 119.6 50.4 41 B GLN CB 895 173.7 120.4 49.6 42 B GLN CG 895 172.7 121.1 50.4 43 B GLN CD 895 171.9 120.1 51.2 44 B GLN OE1 895 170.9 119.5 50.8 44 B GLN NE2 895 172.3 119.9 52.5 45 B LN C 895 175.6 118.8 49.5 40 B GLN O 895 176.6 119.2 48.9 41 B PRO N 896 175.2 117.5 49.3 39 B PRO CD 896 174.1 116.8 49.9 38 B PRO CA 896 176.0 116.6 48.4 38 B PRO CB 896 175.5 115.2 48.8 38 B PRO CG 896 174.0 115.5 49.0 38 B PRO C 896 175.9 116.9 46.9 37 B PRO O 896 174.9 117.5 46.5 37 B THR N 897 176.9 116.5 46.2 36 B THR CA 897 177.0 116.7 44.8 34 B THR CB 897 178.1 117.8 44.4 35 B THR OG1 897 178.0 118.2 43.0 36 B THR CG2 897 179.5 117.3 44.7 33 B THR C 897 177.3 115.4 44.1 32 B THR O 897 178.1 114.6 44.5 32 B HIS N 898 176.6 115.2 42.9 31 B HIS CA 898 176.8 114.0 42.1 31 B HIS CB 898 175.7 113.9 41.1 31 B HIS CG 898 175.5 112.6 40.4 32 B HIS CD2 898 174.4 111.8 40.2 32 B HIS ND1 898 176.6 111.9 39.8 32 B HIS CE1 898 176.1 110.8 39.3 31 B HIS NE2 898 174.8 110.7 39.5 32 B HIS C 898 178.2 114.1 41.5 31 B HIS O 898 178.4 115.0 40.7 31 B PRO N 899 179.1 113.1 41.7 30 B PRO CD 899 178.9 111.9 42.5 31 B PRO CA 899 180.4 113.1 41.1 31 B PRO CB 899 181.1 112.0 41.8 31 B PRO CG 899 180.0 111.0 42.0 32 B PRO C 899 180.6 113.0 39.6 30 B PRO O 899 181.7 113.3 39.1 31 B VAL N 900 179.5 112.8 38.9 28 B VAL CA 900 179.6 112.7 37.4 26 B VAL CB 900 178.7 111.5 36.8 24 B VAL CG1 900 178.6 111.5 35.3 22 B VAL CG2 900 179.3 110.2 37.3 23 B VAL C 900 179.1 114.0 36.8 26 B VAL O 900 179.8 114.6 36.0 26 B TYR N 901 177.9 114.5 37.3 26 B TYR CA 901 177.3 115.7 36.8 26 B TYR CB 901 175.8 115.5 36.7 25 B TYR CG 901 175.3 114.4 35.8 26 B TYR CD1 901 175.0 113.1 36.3 27 B TYR CE1 901 174.6 112.1 35.5 27 B TYR CD2 901 175.2 114.6 34.5 27 B TYR CE2 901 174.8 113.5 33.6 27 B TYR CZ 901 174.5 112.3 34.1 26 B TYR OH 901 174.1 111.2 33.3 24 B TYR C 901 177.6 117.0 37.6 27 B TYR O 901 177.4 118.1 37.0 27 B ASN N 902 178.0 116.8 38.8 28 B ASN CA 902 178.3 117.9 39.7 29 B ASN CB 902 179.5 118.8 39.2 30 B ASN CG 902 180.1 119.6 40.3 30 B ASN OD1 902 180.0 119.2 41.5 30 B ASN ND2 902 180.7 120.7 40.0 30 B ASN C 902 177.1 118.8 39.9 29 B ASN O 902 177.2 120.0 39.7 30 B ILE N 903 176.0 118.2 40.3 30 B ILE CA 903 174.8 118.9 40.6 30 B ILE CB 903 173.8 119.1 39.4 29 B ILE CG2 903 174.5 119.8 38.3 28 B ILE CG1 903 173.2 117.8 38.9 28 B ILE CD1 903 172.1 118.0 37.9 27 B ILE C 903 174.2 117.9 41.6 32 B ILE O 903 174.6 116.7 41.7 33 B GLY N 904 173.3 11a.4 42.5 35 B GLY CA 904 172.7 117.6 43.6 36 B GLY C 904 172.2 116.3 43.1 36 B GLY O 904 171.6 116.2 42.0 37 B PRO N 905 172.6 115.2 43.8 35 B PRO CD 905 173.4 115.3 45.0 35 B PRO CA 905 172.2 113.8 43.5 36 B PRO CB 905 172.6 113.1 44.7 35 B PRO CG 905 173.8 113.8 45.2 35 B PRO C 905 170.7 113.7 43.2 38 B PRO O 905 170.3 112.9 42.3 39 B ASP N 906 169.9 114.5 43.9 40 B ASP CA 906 168.5 114.5 43.7 42 B ASP CB 906 167.9 115.3 44.9 45 B ASP CG 906 168.6 116.6 45.2 48 B ASP OD1 906 169.6 116.6 45.9 51 B ASP OD2 906 168.1 117.7 44.8 50 B ASP C 906 168.0 115.2 42.4 42 B ASP O 906 167.0 114.9 41.9 42 B LYS N 907 168.8 116.2 42.0 41 B LYS CA 907 168.6 116.9 40.8 41 B LYS CB 907 169.4 118.1 40.6 41 B LYS CG 907 169.1 119.2 41.7 41 B LYS CD 907 167.7 119.6 41.6 42 B LYS CE 907 167.3 120.5 42.7 43 B LYS NZ 907 166.0 121.2 42.5 44 B LYS C 907 168.8 115.9 39.6 40 B LYS O 907 168.1 115.9 38.6 40 B VAL N 908 169.9 115.1 39.8 40 B VAL CA 908 170.2 114.1 38.7 41 B VAL CB 908 171.4 113.3 39.1 40 B VAL CG1 908 171.6 112.2 38.2 41 B VAL CG2 908 172.7 114.2 39.1 40 B VAL C 908 169.0 113.2 38.6 42 B VAL O 908 168.4 113.1 37.6 42 B ILE N 909 168.6 112.6 39.7 41 B ILE CA 909 167.5 111.7 39.8 42 B ILE CB 909 167.2 111.2 41.2 41 B ILE CG2 909 165.9 110.3 41.2 41 B ILE CG1 909 168.4 110.4 41.7 41 B ILE CD1 909 168.4 110.1 43.2 41 B ILE C 909 166.2 112.4 39.2 42 B ILE O 909 165.6 111.9 38.2 44 B GLN N 910 165.9 113.5 39.8 42 B GLN CA 910 164.7 114.2 39.4 42 B GLN CB 910 164.6 115.6 40.1 44 B GLN CG 910 163.3 116.3 39.9 46 B GLN CD 910 163.3 117.6 40.7 47 B GLN OE1 910 162.5 118.5 40.4 47 B GLN NE2 910 164.1 117.8 41.7 48 B GLN C 910 164.7 114.5 37.8 42 B GLN O 910 163.7 114.2 37.1 42 B ALA N 911 165.8 115.0 37.3 42 B ALA CA 911 165.8 115.3 35.9 41 B ALA CB 911 167.1 116.1 35.5 41 B ALA C 911 165.8 114.1 35.0 40 B ALA O 911 165.0 114.1 34.0 39 B THR N 912 166.5 113.0 35.3 41 B THR CA 912 166.6 111.8 34.5 42 B THR CB 912 167.6 110.8 35.0 42 B THR OG1 912 167.3 110.4 36.3 44 B THR CG2 912 169.0 111.5 35.0 42 B THR C 912 165.2 111.1 34.4 42 B THR O 912 164.8 110.8 33.3 43 B THR N 913 164.6 110.9 35.5 42 B THR CA 913 163.2 110.2 35.4 41 B THR CB 913 162.7 109.8 36.8 40 B THR OG1 913 161.8 110.7 37.3 41 B THR CG2 913 163.9 109.5 37.8 41 B THR C 913 162.2 111.1 34.7 40 B THR O 913 161.3 110.6 34.0 41 B HIS N 914 162.3 112.4 34.8 38 B HIS CA 914 161.4 113.3 34.1 37 B HIS CB 914 161.5 114.7 34.6 36 B HIS CG 914 160.8 115.7 33.7 34 B HIS CD2 914 159.6 116.2 33.8 34 B HIS ND1 914 161.3 116.1 32.5 34 B HIS CE1 914 160.4 116.9 31.9 33 B HIS NE2 914 159.3 116.9 32.6 34 B HIS C 914 161.5 113.2 32.6 38 B HIS O 914 160.5 113.2 31.9 38 B PHE N 915 162.7 113.2 32.1 39 B PHE CA 915 163.0 113.2 30.7 38 B PHE CB 915 164.4 113.7 30.4 37 B PHE CG 915 164.5 115.2 30.5 35 B PHE CD1 915 165.2 115.7 31.5 35 B PHE CD2 915 164.0 116.0 29.5 35 B PHE CE1 915 165.3 117.1 31.6 35 B PHE CE2 915 164.0 117.4 29.6 34 B PHE CZ 915 164.7 117.9 30.7 34 B PHE C 915 162.7 111.8 30.1 39 B PHE O 915 162.6 111.6 28.9 39 B LEU N 916 162.7 110.8 31.0 41 B LEU CA 916 162.4 109.5 30.7 43 B LEU CB 916 162.8 108.5 31.9 43 B LEU CG 916 164.0 107.7 31.8 43 B LEU CD1 916 165.0 108.2 30.7 44 B LEU CD2 916 164.7 107.5 33.1 43 B LEU C 916 161.0 109.3 30.2 45 B LEU O 916 160.7 108.5 29.4 45 B GLN N 917 160.1 110.2 30.7 46 B GLN CA 917 158.7 110.2 30.3 48 B GLN CB 917 157.9 111.3 31.0 50 B GLN CG 917 158.0 111.4 32.5 53 B GLN CD 917 157.5 112.7 33.0 54 B GLN OE1 917 158.1 113.4 33.8 57 B GLN NE2 917 156.4 113.2 32.5 55 B GLN C 917 158.6 110.5 28.8 48 B GLN O 917 157.6 110.3 28.2 48 B LYS N 918 159.7 111.1 28.3 49 B LYS CA 918 159.7 111.4 26.9 50 B LYS CB 918 160.4 112.8 26.7 50 B LYS CG 918 159.6 113.9 27.4 51 B LYS CD 918 160.0 114.1 28.9 50 B LYS CE 918 158.9 114.9 29.6 50 B LYS NZ 918 158.6 116.2 28.9 50 B LYS C 918 160.5 110.4 26.1 51 B LYS O 918 161.4 109.7 26.6 51 B PRO N 919 160.1 110.1 24.8 52 B PRO CD 919 159.0 110.6 24.0 52 B PRO CA 919 160.9 109.1 24.1 53 B PRO CB 919 159.9 108.7 23.0 52 B PRO CG 919 159.3 110.0 22.7 52 B PRO C 919 162.1 109.8 23.5 54 B PRO O 919 162.1 111.0 23.3 54 B VAL N 920 163.2 109.0 23.4 55 B VAL CA 920 164.4 109.5 22.7 56 B VAL CB 920 165.4 108.4 22.5 55 B VAL CG1 920 166.6 108.8 21.7 54 B VAL CG2 920 165.9 107.8 23.9 53 B VAL C 920 163.9 110.0 21.4 60 B VAL O 920 163.2 109.3 20.7 60 B PRO N 921 164.3 111.3 21.0 63 B PRO CD 921 165.0 112.3 21.7 63 B PRO CA 921 163.9 111.8 19.6 66 B PRO CB 921 164.7 113.1 19.5 64 B PRO CG 921 164.8 113.6 20.9 63 B PRO C 921 164.1 110.8 18.5 69 B PRO O 921 165.2 110.7 18.0 69 B GLY N 922 163.1 110.0 18.3 74 B GLY CA 922 163.2 108.9 17.3 80 B GLY C 922 163.0 109.3 15.8 84 B GLY O 922 162.6 110.4 15.5 85 B PHE N 923 163.4 108.3 15.0 88 B PHE CA 923 163.3 108.5 13.5 91 B PHE CB 923 164.8 108.5 13.0 93 B PHE CG 923 165.8 109.0 13.9 94 B PHE CD1 923 166.1 110.3 14.0 95 B PHE CD2 923 166.5 108.1 14.8 95 B PHE CE1 923 167.1 110.8 14.9 95 B PHE CE2 923 167.4 108.6 15.7 95 B PHE CZ 923 167.8 109.9 15.7 95 B PHE C 923 162.5 107.4 13.0 92 B PHE OT1 923 163.0 106.2 13.0 93 B PHE OT2 923 161.3 107.6 12.8 93 B ZIN ZN 1000 191.8 126.9 39.0 28 Z FPP P 2001 197.0 126.1 33.2 22 F FPP O 2001 196.9 127.7 33.2 22 F FPP 01 2001 198.5 125.8 32.7 22 F FPP 02 2001 196.7 125.5 34.6 24 F FPP 03 2001 196.0 125.5 32.1 22 F FPP C 2001 195.9 124.2 31.7 22 F FPP C1 2001 193.8 123.3 30.4 22 F FPP C2 2001 194.4 123.7 31.5 22 F FPP C3 2001 192.4 122.7 30.4 22 F FPP C4 2001 194.4 123.4 29.0 21 F FPP C5 2001 191.8 122.4 31.8 22 F FPP C6 2001 189.4 122.1 32.6 20 F FPP C7 2001 190.4 121.8 31.7 21 F FPP C8 2001 189.5 123.1 33.7 20 F FPP C9 2001 188.2 121.2 32.6 19 F FPP C10 2001 187.0 121.9 31.9 18 F FPP C11 2001 185.7 121.1 32.0 17 F FPP C12 2001 184.6 121.4 31.4 17 F FPP C13 2001 184.4 122.6 30.5 18 F FPP C14 2001 183.4 120.5 31.5 17 F FPP P1 2001 197.6 124.4 35.2 24 F FPP 04 2001 196.9 124.0 36.6 24 F FPP 05 2001 197.6 123.1 34.3 24 F FPP 06 2001 199.0 124.9 35.5 24 F SCH C1 2002 184.9 127.1 32.3 26 I SCH N2 2002 185.7 128.1 31.9 26 I SCH C3 2002 187.0 128.1 32.3 25 I SCH C4 2002 187.6 127.1 33.1 25 I SCH C5 2002 186.7 126.1 33.5 25 I SCH C6 2002 185.4 126.1 33.1 25 I SCH C9 2002 187.8 129.2 31.8 26 I SCH C10 2002 189.0 128.9 30.9 25 I SCH C11 2002 189.9 127.9 31.2 27 I SCH C12 2002 190.0 126.9 32.4 26 I SCH C13 2002 189.0 127.2 33.5 26 I SCH C18 2002 189.1 129.7 29.8 24 I SCH C19 2002 190.1 129.5 28.9 26 I SCH C20 2002 191.1 128.5 29.1 27 I SCH C21 2002 191.0 127.7 30.3 27 I SCH C24 2002 188.3 130.2 33.0 27 I SCH C25 2002 188.4 131.6 32.5 27 I SCH C26 2002 188.6 132.7 33.6 29 I SCH N27 2002 187.8 132.5 34.8 30 I SCH C28 2002 187.7 131.1 35.3 30 I SCH C29 2002 187.3 130.1 34.2 28 I SCHBR38 2002 184.2 124.7 33.7 28 I SCHBR39 2002 192.3 126.4 30.6 31 I SCHCL40 2002 192.4 128.2 28.1 25 I SCH C41 2002 187.2 133.5 35.4 30 I SCH 042 2002 186.5 133.4 36.4 33 I SCH C43 2002 187.5 134.9 34.9 31 I SCH C44 2002 187.2 136.0 35.9 30 I SCH C47 2002 187.1 137.4 35.3 30 I SCH C48 2002 187.1 138.6 36.3 30 I SCH N49 2002 188.1 138.4 37.3 31 I SCH C50 2002 188.0 137.1 38.1 30 I SCH C51 2002 188.2 136.0 37.1 30 I SCH C61 2002 189.1 139.2 37.6 33 I SCH 062 2002 190.0 138.9 38.3 35 I SCH N63 2002 189.0 140.4 36.9 34 I HOH OH2 1001 195.7 134.3 28.0 21 W HOH OH2 1002 188.3 129.9 17.0 15 W HOH OH2 1003 202.0 124.3 44.4 17 W HOH OH2 1004 203.6 117.7 25.9 14 W HOH OH2 1005 198.5 115.4 20.3 19 W HOH OH2 1006 188.9 124.1 29.9 18 W HOH OH2 1007 200.2 114.9 34.8 16 W HOH OH2 1008 185.9 127.8 28.3 24 W HOH OH2 1009 192.7 123.5 18.2 23 W HOH OH2 1010 198.3 126.1 29.8 16 W HOH OH2 1011 197.4 117.7 19.3 17 W HOH OH2 1012 205.3 120.2 34.9 16 W HOH OH2 1013 189.2 130.4 25.4 17 W HOH OH2 1014 192.1 125.3 20.7 19 W HOH OH2 1015 186.7 125.5 28.8 22 W HOH OH2 1046 203.0 109.6 23.6 23 W HOH OH2 1017 184.6 130.1 30.4 25 W HOH OH2 1018 193.9 124.3 22.5 20 W HOH OH2 1019 194.6 119.0 18.9 23 W HOH OH2 1020 180.1 133.7 21.3 20 W HOH OH2 1021 203.8 120.4 32.7 18 W HOH OH2 1022 207.4 126.4 33.4 25 W HOH OH2 1023 204.4 127.6 36.9 26 W HOH OH2 1024 181.7 104.6 22.8 27 W HOH OH2 1025 191.7 121.8 22.7 27 W HOH OH2 1026 178.3 138.0 20.2 30 W HOH OH2 1027 186.2 126.7 23.9 21 W HOH OH2 1028 200.2 125.5 37.8 22 W HOH OH2 1029 188.3 136.9 26.9 28 W HOH OH2 1030 200.0 132.8 29.9 28 W HOH OH2 1031 182.4 129.5 26.2 27 W HOH OH2 1032 205.7 125.0 37.1 27 W HOH OH2 1033 198.2 103.7 28.2 38 W HOH OH2 1034 203.8 119.9 48.2 26 W HOH OH2 1035 195.9 127.4 29.4 25 W HOH OH2 1036 183.5 127.3 27.5 30 W HOH OH2 1037 180.9 120.8 36.7 28 W HOH OH2 1038 190.7 120.8 17.0 31 W HOH OH2 1039 210.0 125.3 33.1 21 W HOH OH2 1040 198.4 122.5 38.2 21 W HOH OH2 1041 201.1 130.7 28.8 21 W HOH OH2 1042 192.9 121.5 45.2 26 W HOH OH2 1043 201.4 127.9 36.7 34 W HOH OH2 1044 194.2 139.9 8.6 22 W HOH OH2 1045 192.1 118.4 18.4 24 W HOH OH2 1046 202.1 115.3 46.7 34 W HOH OH2 1047 190.2 132.1 37.4 30 W HOH OH2 1048 189.4 132.3 27.3 29 W HOH OH2 1049 190.8 134.8 26.7 31 W HOH OH2 1050 180.2 127.9 15.7 32 W HOH OH2 1051 190.3 139.4 25.4 37 W HOH OH2 1052 206.5 133.6 14.1 30 W HOH OH2 1053 186.9 129.2 25.4 23 W HOH OH2 1054 191.5 116.0 17.4 30 W HOH OH2 1055 194.2 139.4 5.7 21 W HOH OH2 1056 184.1 132.3 27.3 28 W HOH OH2 1057 200.9 126.4 31.4 26 W HOH OH2 1058 201.8 128.9 33.9 36 W HOH OH2 1059 192.4 131.0 32.5 31 W HOH OH2 1060 184.6 130.9 25.1 22 W HOH OH2 1061 176.2 138.0 26.3 28 W HOH OH2 1062 193.6 121.5 24.9 28 W HOH OH2 1063 202.9 139.3 14.3 32 W HOH OH2 1064 195.8 113.6 18.6 31 W HOH OH2 1065 207.7 124.8 11.6 24 W HOH OH2 1066 179.3 139.3 43.4 31 W HOH OH2 1067 185.6 130.0 16.5 27 W HOH OH2 1068 186.7 126.1 10.3 34 W HOH OH2 1069 191.9 136.7 37.9 34 W HOH OH2 1070 185.7 114.5 21.9 22 W HOH OH2 1071 207.2 108.9 11.3 37 W HOH OH2 1072 196.1 126.3 38.0 24 W HOH OH2 1073 201.9 111.1 25.6 24 W HOH OH2 1074 201.0 107.7 25.9 33 W HOH OH2 1075 211.9 126.6 31.8 25 W HOH OH2 1076 207.5 134.5 17.0 33 W HOH OH2 1077 204.3 112.7 35.1 26 W HOH OH2 1078 208.1 128.8 31.9 24 W HOH OH2 1079 187.7 134.2 29.9 32 W HOH OH2 1080 187.6 112.2 12.6 34 W HOH OH2 1081 203.7 111.6 11.6 32 W HOH OH2 1082 178.2 126.1 16.8 34 W HOH OH2 1083 192.6 132.5 30.4 39 W HOH OH2 1084 174.9 122.4 14.5 29 W HOH OH2 1085 203.2 127.9 9.2 20 W HOH OH2 1086 192.4 132.6 39.4 27 W HOH OH2 1087 208.5 137.2 22.2 48 W HOH OH2 1088 183.9 133.3 37.3 35 W HOH OH2 1089 212.1 129.9 29.3 34 W HOH OH2 1090 179.3 103.2 34.5 36 W HOH OH2 1091 185.0 128.3 11.2 36 W HOH OH2 1092 212.5 125.8 29.3 25 W HOH OH2 1093 201.7 110.0 39.1 35 W HOH OH2 1094 192.5 126.8 35.8 34 W HOH OH2 1095 199.2 109.1 24.5 34 W HOH OH2 1096 187.9 124.2 12.1 33 W HOH OH2 1097 190.7 103.0 22.2 32 W HOH OH2 1098 185.2 158.5 8.1 42 W HOH OH2 1099 187.2 127.8 18.2 30 W HOH OH2 1100 187.5 124.9 8.1 45 W HOH OH2 1101 191.4 132.1 41.9 27 W HOH OH2 1102 201.1 137.1 27.9 52 W HOH OH2 1103 192.3 141.9 18.2 34 W HOH OH2 1104 213.6 113.9 16.5 30 W HOH OH2 1105 204.4 118.0 41.4 29 W HOH OH2 1106 188.1 106.4 46.2 29 W HOH OH2 1107 179.1 115.3 47.8 34 W HOH OH2 1108 190.4 134.8 39.6 25 W HOH OH2 1109 189.3 101.2 23.8 42 W HOH OH2 1110 204.6 130.6 42.5 29 W HOH OH2 1111 211.6 123.4 30.0 26 W HOH OH2 1112 177.0 127.9 13.1 37 W HOH OH2 1113 200.4 107.2 44.1 36 W HOH OH2 1114 186.9 98.8 21.9 41 W HOH OH2 1115 198.5 142.5 12.8 47 W HOH OH2 1116 174.9 118.7 31.8 27 W HOH OH2 1117 220.9 119.9 25.1 38 W HOH OH2 1118 208.9 132.7 48.8 41 W HOH OH2 1119 175.2 108.3 35.5 40 W HOH OH2 1120 182.8 100.1 23.2 42 W HOH OH2 1121 201.5 132.1 32.9 48 W HOH OH2 1122 197.6 114.9 15.1 38 W HOH OH2 1123 211.1 127.7 27.8 29 W HOH OH2 1124 162.9 134.0 25.3 39 W HOH OH2 1125 213.9 127.7 21.6 37 W HOH OH2 1126 220.3 126.0 32.0 48 W HOH OH2 1127 199.0 103.3 31.6 35 W HOH OH2 1128 210.7 135.2 24.4 40 W HOH OH2 1129 201.4 108.1 22.0 45 W HOH OH2 1130 172.4 144.0 28.1 37 W HOH OH2 1131 195.5 111.4 47.4 31 W HOH OH2 1132 202.4 109.2 13.1 50 W HOH OH2 1133 215.0 130.3 29.5 39 W HOH OH2 1134 212.0 124.5 17.4 34 W HOH OH2 1135 189.1 114.6 16.2 34 W HOH OH2 1136 168.5 122.8 22.2 29 W HOH OH2 1137 177.9 141.2 24.4 33 W HOH OH2 1138 219.4 124.1 26.2 45 W HOH OH2 1139 195.1 141.5 4.4 36 W HOH OH2 1140 211.3 120.0 16.0 29 W HOH OH2 1141 181.7 139.1 23.9 32 W HOH OH2 1142 178.0 111.9 46.4 57 W HOH OH2 1143 185.8 151.8 10.3 36 W HOH OH2 1144 172.6 139.1 17.9 44 W HOH OH2 1145 215.2 102.2 15.8 43 W HOH OH2 1146 214.1 107.1 19.7 33 W HOH OH2 1147 218.4 123.1 49.2 44 W HOH OH2 1148 200.9 96.8 26.4 50 W HOH OH2 1149 211.2 133.4 16.9 44 W HOH OH2 1150 203.4 135.4 11.0 36 W HOH OH2 1151 178.2 141.2 41.7 34 W HOH OH2 1152 221.1 124.3 40.7 49 W HOH OH2 1153 184.0 135.1 27.0 29 W HOH OH2 1154 191.9 133.7 36.2 62 W HOH OH2 1155 195.9 123.9 17.9 29 W HOH OH2 1156 175.1 101.7 16.1 47 W HOH OH2 1157 203.6 135.6 7.7 38 W HOH OH2 1158 189.6 107.1 17.8 40 W HOH OH2 1159 177.2 144.0 24.6 30 W HOH OH2 1160 196.4 123.9 20.9 26 W HOH OH2 1161 205.2 103.6 15.1 64 W HOH OH2 1162 172.1 121.8 14.4 36 W HOH OH2 1163 194.1 143.8 17.6 42 W HOH OH2 1164 194.3 141.0 1.6 39 W HOH OH2 1165 214.4 127.7 33.0 34 W HOH OH2 1166 211.0 129.1 31.6 30 W HOH OH2 1167 179.3 120.7 11.7 48 W HOH OH2 1168 205.3 122.0 41.5 29 W HOH OH2 1169 170.0 142.6 37.6 41 W HOH OH2 1170 205.7 118.3 45.8 46 W HOH OH2 1171 202.4 120.9 3.1 50 W HOH OH2 1172 216.3 115.3 17.3 33 W HOH OH2 1173 208.6 116.8 41.5 36 W HOH OH2 1174 218.9 125.1 46.6 52 W HOH OH2 1175 157.0 125.0 36.3 41 W HOH OH2 1176 206.4 130.8 33.0 33 W HOH OH2 1177 206.3 119.2 48.5 41 W HOH OH2 1178 204.4 132.7 13.1 34 W HOH OH2 1179 191.2 100.7 25.7 45 W HOH OH2 1180 193.7 130.2 38.5 48 W HOH OH2 1181 172.8 130.2 16.3 43 W HOH OH2 1182 159.9 126.5 29.7 41 W HOH OH2 1183 207.9 122.8 7.1 42 W HOH OH2 1184 215.5 121.5 17.4 41 W HOH OH2 1185 204.1 127.5 33.6 39 W HOH OH2 1186 192.1 144.1 6.6 45 W HOH OH2 1187 207.0 137.1 17.1 57 W HOH OH2 1188 212.1 90.1 38.0 44 W HOH OH2 1189 201.5 105.9 19.3 56 W HOH OH2 1190 205.4 136.6 12.5 48 W HOH OH2 1191 177.6 133.6 8.1 37 W HOH OH2 1192 198.3 126.5 39.4 33 W HOH OH2 1193 187.4 141.5 31.1 31 W HOH OH2 1194 205.9 124.2 39.8 35 W HOH OH2 1195 205.5 103.4 26.6 45 W HOH OH2 1196 176.5 151.9 22.0 47 W HOH OH2 1197 188.2 114.7 13.3 48 W HOH OH2 1198 204.9 138.7 24.2 41 W HOH OH2 1199 186.7 131.8 29.0 39 W HOH OH2 1200 194.5 118.3 9.7 55 W HOH OH2 1201 160.4 118.0 26.8 51 W HOH OH2 1202 186.1 122.4 13.3 41 W HOH OH2 1203 181.4 147.9 35.9 38 W HOH OH2 1204 189.3 120.5 14.5 48 W HOH OH2 1205 173.4 108.1 39.7 55 W HOH OH2 1206 216.7 122.8 19.7 40 W HOH OH2 1207 207.1 120.0 42.1 39 W HOH OH2 1208 213.8 117.9 43.6 36 W HOH OH2 1209 211.4 127.4 23.1 36 W HOH OH2 1210 193.6 116.9 16.0 41 W HOH OH2 1211 191.5 123.3 65.6 49 W HOH OH2 1212 178.6 142.2 45.4 50 W HOH OH2 1213 182.5 99.9 31.8 39 W HOH OH2 1214 211.4 120.7 10.9 47 W HOH OH2 1215 209.3 127.0 12.3 33 W HOH OH2 1216 211.5 130.4 18.5 38 W HOH OH2 1217 165.4 105.5 27.3 51 W HOH OH2 1218 193.9 128.8 33.1 41 W HOH OH2 1219 190.6 122.7 5.9 43 W HOH OH2 1220 209.8 116.6 47.5 45 W HOH OH2 1221 196.7 107.4 19.1 52 W HOH OH2 1222 183.8 158.5 20.1 34 W HOH OH2 1223 215.7 128.2 24.5 55 W HOH OH2 1224 175.1 145.8 5.0 47 W HOH OH2 1225 200.8 105.3 36.7 40 W HOH OH2 1226 191.3 142.8 10.8 42 W HOH OH2 1227 157.5 122.3 38.9 58 W HOH OH2 1228 210.8 130.8 38.5 40 W HOH OH2 1229 209.6 123.1 9.8 42 W HOH OH2 1230 196.6 119.6 6.9 48 W HOH OH2 1231 175.1 141.0 30.1 35 W HOH OH2 1232 190.0 159.7 15.0 42 W HOH OH2 1233 172.1 118.0 46.7 37 W HOH OH2 1234 162.7 119.4 27.6 40 W HOH OH2 1235 208.8 98.3 25.8 52 W HOH OH2 1236 202.0 100.9 43.9 38 W HOH OH2 1237 209.2 131.4 36.1 43 W HOH OH2 1238 185.7 149.3 10.1 38 W HOH OH2 1239 212.0 125.6 12.7 46 W HOH OH2 1240 213.0 109.0 18.2 39 W HOH OH2 1241 218.0 120.9 34.6 49 W HOH OH2 1242 212.3 95.1 26.6 47 W HOH OH2 1243 192.9 146.6 23.8 53 W HOH OH2 1244 189.9 145.2 26.6 56 W HOH OH2 1245 169.1 108.3 26.3 39 W HOH OH2 1246 170.5 147.1 12.2 56 W HOH OH2 1247 195.4 108.8 48.1 37 W HOH OH2 1248 211.4 118.7 13.7 36 W HOH OH2 1249 201.6 114.9 53.7 37 W HOH OH2 1250 187.0 149.7 6.3 48 W HOH OH2 1251 217.1 128.4 31.3 55 W HOH OH2 1252 180.0 127.2 58.1 39 W HOH OH2 1253 202.9 103.1 28.9 41 W HOH OH2 1254 213.5 123.4 13.5 48 W HOH OH2 1255 196.2 116.2 17.3 55 W HOH OH2 1256 196.9 143.3 17.1 58 W HOH OH2 1257 213.8 126.4 19.0 48 W HOH OH2 1258 175.8 138.7 21.9 55 W HOH OH2 1259 183.0 158.8 22.8 43 W HOH OH2 1260 212.3 118.9 53.4 45 W HOH OH2 1261 204.2 138.7 6.1 55 W HOH OH2 1262 185.5 127.5 20.9 34 W HOH OH2 1263 200.6 141.7 8.4 54 W HOH OH2 1264 203.3 134.7 25.5 39 W HOH OH2 1265 219.5 123.6 37.2 48 W HOH OH2 1266 204.2 132.5 32.5 53 W HOH OH2 1267 211.3 109.9 12.2 44 W HOH OH2 1268 192.1 113.4 18.0 45 W HOH OH2 1269 184.3 98.6 28.0 50 W HOH OH2 1270 169.6 121.6 47.1 68 W HOH OH2 1271 210.6 125.5 8.8 50 W HOH OH2 1272 180.5 140.5 48.1 54 W HOH OH2 1273 200.0 109.5 19.4 56 W HOH OH2 1274 199.7 107.7 58.8 51 W HOH OH2 1275 205.3 118.6 5.8 43 W HOH OH2 1276 207.2 115.9 5.7 46 W HOH OH2 1277 171.7 131.5 20.7 39 W HOH OH2 1278 161.2 127.6 37.2 47 W HOH OH2 1279 212.6 102.9 53.5 54 W HOH OH2 1280 194.2 135.9 40.1 44 W HOH OH2 1281 221.6 113.4 44.5 55 W HOH OH2 1282 190.2 140.7 30.9 60 W HOH OH2 1283 172.5 148.6 25.3 56 W HOH OH2 1284 177.6 110.8 52.9 44 W HOH OH2 1285 203.9 115.7 42.8 49 W HOH OH2 1286 169.0 105.5 26.1 57 W HOH OH2 1287 192.6 124.0 2.2 51 W HOH OH2 1288 174.0 145.7 24.9 42 W HOH OH2 1289 197.3 111.6 25.9 33 W HOH OH2 1290 166.5 118.1 38.0 33 W HOH OH2 1291 181.2 141.4 39.7 48 W HOH OH2 1292 212.6 127.9 25.6 40 W HOH OH2 1293 191.1 134.2 1.8 40 W HOH OH2 1294 199.2 129.2 37.5 60 W HOH OH2 1295 189.7 110.1 53.2 41 W HOH OH2 1296 179.2 131.6 58.4 52 W HOH OH2 1297 204.0 96.4 34.8 57 W HOH OH2 1298 210.9 120.8 56.3 55 W HOH OH2 1299 206.0 129.3 3.1 61 W HOH OH2 1300 194.0 142.3 9.6 48 W HOH OH2 1301 195.3 113.3 60.3 52 W HOH OH2 1302 180.3 112.8 47.7 55 W HOH OH2 1303 209.1 113.8 48.1 49 W HOH OH2 1304 164.8 126.3 20.2 59 W HOH OH2 1305 219.8 118.8 21.9 52 W HOH OH2 1306 179.2 133.3 10.6 54 W HOH OH2 1307 202.5 109.0 36.6 37 W HOH OH2 1308 162.2 128.0 42.5 56 W HOH OH2 1309 203.8 106.7 35.2 42 W HOH OH2 1310 198.5 118.9 53.9 41 W HOH OH2 1311 217.4 104.5 15.9 53 W HOH OH2 1312 160.6 113.1 21.2 50 W HOH OH2 1313 219.5 104.4 19.6 52 W HOH OH2 1314 214.0 111.2 16.1 45 W HOH OH2 1315 187.6 133.5 55.7 48 W HOH OH2 1316 201.5 104.9 26.4 62 W HOH OH2 1317 206.8 106.0 38.8 53 W HOH OH2 1318 191.4 112.2 55.4 46 W HOH OH2 1319 190.9 130.8 53.0 46 W HOH OH2 1320 188.4 150.6 14.7 46 W HOH OH2 1321 181.3 107.7 14.5 47 W HOH OH2 1322 195.5 147.7 17.4 63 W HOH OH2 1323 199.1 99.5 54.4 52 W HOH OH2 1324 189.3 152.0 27.7 59 W HOH OH2 1325 163.4 120.7 41.4 52 W HOH OH2 1326 206.6 130.9 35.8 45 W HOH OH2 1327 184.0 148.8 37.1 60 W HOH OH2 1328 203.8 139.2 17.2 58 W HOH OH2 1329 187.0 149.4 12.4 51 W HOH OH2 1330 190.4 122.6 12.1 53 W HOH OH2 1331 207.3 106.0 41.7 49 W HOH OH2 1332 200.1 98.4 32.1 70 W HOH OH2 1333 201.5 140.8 20.6 55 W HOH OH2 1334 187.3 124.3 5.4 60 W HOH OH2 1335 184.8 138.3 41.1 47 W HOH OH2 1336 189.8 157.8 22.5 34 W HOH OH2 1337 186.6 147.6 28.0 66 W HOH OH2 1338 202.8 140.6 23.7 58 W HOH OH2 1339 170.4 139.7 21.8 54 W HOH OH2 1340 159.5 121.5 41.4 69 W HOH OH2 1341 187.1 105.8 18.3 42 W HOH OH2 1342 174.7 128.1 14.1 53 W HOH OH2 1343 173.4 135.2 9.1 45 W HOH OH2 1344 184.3 121.0 56.3 41 W HOH OH2 1345 190.3 147.8 14.4 41 W HOH OH2 1346 194.7 121.3 4.8 50 W HOH OH2 1347 176.9 130.9 9.9 63 W HOH OH2 1348 174.0 118.2 54.2 53 W HOH OH2 1349 202.0 131.5 43.1 61 W HOH OH2 1350 175.9 137.5 18.7 50 W HOH OH2 1351 179.9 138.8 50.5 47 W HOH OH2 1352 195.2 114.9 13.3 55 W HOH OH2 1353 198.4 103.4 58.2 47 W HOH OH2 1354 187.5 144.3 31.3 45 W HOH OH2 1355 174.7 124.0 52.8 38 W HOH OH2 1356 184.2 148.4 3.6 56 W HOH OH2 1357 170.1 144.7 27.3 56 W HOH OH2 1358 167.5 142.6 19.8 64 W HOH OH2 1359 162.2 125.8 24.1 52 W HOH OH2 1360 175.5 135.6 10.6 49 W HOH OH2 1361 193.8 115.4 62.4 59 W HOH OH2 1362 177.6 109.6 14.3 70 W HOH OH2 1363 203.0 130.4 6.8 42 W HOH OH2 1364 196.6 101.3 22.1 55 W HOH OH2 1365 156.8 125.3 30.2 57 W HOH OH2 1366 203.7 96.6 38.5 57 W HOH OH2 1367 193.9 130.5 57.4 48 W HOH OH2 1368 180.9 149.6 33.7 61 W HOH OH2 1369 219.1 125.3 34.8 54 W HOH OH2 1370 187.5 144.2 28.0 51 W HOH OH2 1371 183.7 151.1 20.7 39 W HOH OH2 1372 176.3 148.8 29.7 48 W HOH OH2 1373 191.8 142.0 0.7 61 W HOH OH2 1374 214.3 125.3 43.9 44 W HOH OH2 1375 176.9 104.4 21.0 49 W HOH OH2 1376 216.9 112.9 14.1 55 W HOH OH2 1377 197.5 153.1 18.0 56 W HOH OH2 1378 184.6 145.4 1.0 59 W HOH OH2 1379 209.6 120.7 42.2 41 W HOH OH2 1380 184.5 110.0 54.8 38 W HOH OH2 1381 214.9 114.0 37.4 50 W HOH OH2 1382 212.7 122.2 16.4 47 W HOH OH2 1383 187.8 143.4 1.3 57 W HOH OH2 1384 206.9 100.8 20.9 54 W HOH OH2 1385 158.7 131.8 32.0 56 W HOH OH2 1386 174.4 146.8 28.4 55 W HOH OH2 1387 191.2 129.5 35.7 64 W HOH OH2 1388 173.2 135.9 54.4 52 W HOH OH2 1389 218.0 116.4 28.2 59 W HOH OH2 1390 217.1 97.1 26.2 42 W HOH OH2 1391 175.7 125.5 15.2 56 W HOH OH2 1392 207.0 117.2 43.7 58 W HOH OH2 1393 169.1 124.4 46.5 68 W HOH OH2 1394 179.7 134.1 56.6 52 W HOH OH2 1395 169.8 108.4 29.2 55 W HOH OH2 1396 173.8 143.2 4.1 60 W HOH OH2 1397 159.5 118.6 39.2 54 W HOH OH2 1398 190.6 124.9 7.7 53 W HOH OH2 1399 212.3 92.4 39.4 51 W HOH OH2 1400 196.9 142.7 5.8 73 W HOH OH2 1401 212.8 127.2 16.6 55 W HOH OH2 1402 166.2 131.2 21.6 60 W HOH OH2 1403 203.3 132.5 27.3 43 W HOH OH2 1404 177.7 103.3 25.9 55 W HOH OH2 1405 175.0 106.0 21.9 52 W HOH OH2 1406 213.2 130.3 21.4 68 W HOH OH2 1407 214.8 129.1 27.1 65 W HOH OH2 1408 183.9 141.8 39.5 64 W HOH OH2 1409 164.1 128.8 24.2 59 W HOH OH2 1410 216.7 118.7 49.3 59 W HOH OH2 1411 210.9 118.2 42.3 48 W HOH OH2 1412 178.6 148.0 37.5 58 W HOH OH2 1413 185.6 136.2 55.8 56 W HOH OH2 1414 218.9 91.1 39.8 58 W HOH OH2 1415 207.9 131.5 13.5 54 W HOH OH2 1416 204.3 130.2 38.5 61 W HOH OH2 1417 165.9 136.6 32.5 43 W HOH OH2 1418 188.0 141.4 28.3 48 W HOH OH2 1419 207.9 133.3 32.2 67 W HOH OH2 1420 187.2 146.8 31.2 61 W HOH OH2 1421 189.5 104.8 19.3 62 W HOH OH2 1422 208.7 111.0 9.3 63 W HOH OH2 1423 202.4 133.7 59.8 75 W HOH OH2 1424 216.4 127.7 36.3 65 W HOH OH2 1425 217.8 116.9 15.4 53 W HOH OH2 1426 160.4 118.6 29.6 54 W HOH OH2 1427 174.7 133.2 7.4 58 W HOH OH2 1428 181.4 102.2 21.5 62 W HOH OH2 1429 171.7 109.9 34.7 66 W HOH OH2 1430 197.8 111.1 58.3 74 W HOH OH2 1431 183.9 105.6 11.6 52 W HOH OH2 1432 195.3 153.9 15.5 62 W HOH OH2 1433 202.0 138.1 3.0 48 W HOH OH2 1434 194.9 148.2 21.5 60 W HOH OH2 1435 204.3 111.4 54.3 54 W HOH OH2 1436 216.4 107.6 18.0 65 W HOH OH2 1437 174.7 145.5 31.2 59 W HOH OH2 1438 182.0 156.5 25.2 66 W

TABLE 4 The following table lists the atomic structure coordinates for FPT in complex with FPP and the inhibitor SCH66701 as derived by X-ray diffraction from crystals of that complex The abbreviations are the same as those used in Table 2 RES ATOM # X Y Z B C GLY C 54 192.9 151.9 9.4 80 A GLY O 54 191.7 151.8 9.5 81 A GLY N 54 193.8 151.4 7.1 80 A GLY CA 54 193.5 152.5 8.1 80 A PHE N 55 193.8 151.5 10.3 80 A PHE CA 55 193.4 150.9 11.5 78 A PHE CB 55 194.3 149.7 11.8 79 A PHE CG 55 193.7 148.4 11.3 80 A PHE CD1 55 194.2 147.8 10.1 80 A PHE CD2 55 192.7 147.7 12.0 80 A PHE CE1 55 193.7 146.6 9.7 80 A PHE CE2 55 192.2 146.5 11.5 80 A PHE CZ 55 192.7 145.9 10.4 80 A PHE C 55 193.5 151.8 12.7 77 A PHE O 55 194.6 152.3 13.1 77 A LEU N 56 192.4 152.1 13.4 74 A LEU CA 56 192.4 152.9 14.6 71 A LEU CB 56 191.3 153.9 14.6 72 A LEU CG 56 191.6 155.4 14.8 73 A LEU CD1 56 190.4 156.3 14.8 73 A LEU CD2 56 192.4 155.6 16.1 72 A LEU C 56 192.5 152.1 15.8 69 A LEU O 56 191.6 151.4 16.2 69 A SER N 57 193.7 152.1 16.4 66 A SER CA 57 194.0 151.3 17.6 64 A SER CB 57 195.4 151.6 18.1 64 A SER OG 57 195.8 150.9 19.3 64 A SER C 57 193.0 151.5 18.7 62 A SER O 57 192.5 152.6 19.0 61 A LEU N 58 192.6 150.4 19.4 59 A LEU CA 58 191.7 150.5 20.5 57 A LEU CB 58 191.3 149.1 21.0 56 A LEU CG 58 189.9 148.6 20.9 56 A LEU CD1 58 189.8 147.2 21.4 56 A LEU CD2 58 188.9 149.5 21.6 55 A LEU C 58 192.4 151.2 21.6 57 A LEU O 58 191.8 151.7 22.6 57 A ASP N 59 193.7 151.3 21.5 57 A ASP CA 59 194.6 152.0 22.4 56 A ASP CB 59 195.9 151.2 22.6 60 A ASP CG 59 195.7 150.0 23.6 62 A ASP OD1 59 195.1 149.0 23.2 62 A ASP OD2 59 196.2 150.1 24.7 62 A ASP C 59 195.0 153.4 22.0 54 A ASP O 59 195.6 154.2 22.8 54 A SER N 60 194.7 153.8 20.8 51 A SER CA 60 195.0 155.1 20.2 48 A SER CB 60 194.5 155.2 18.8 47 A SER OG 60 194.9 156.4 18.3 47 A SER C 60 194.5 156.2 21.1 46 A SER O 60 193.3 156.1 21.5 46 A PRO N 61 195.3 157.2 21.4 44 A PRO CD 61 196.6 157.5 20.8 43 A PRO CA 61 194.8 158.3 22.2 43 A PRO CB 61 196.0 159.2 22.4 43 A PRO CG 61 196.7 159.0 21.1 43 A PRO C 61 193.7 159.0 21.5 41 A PRO O 61 192.9 159.8 22.1 40 A THR N 62 193.6 158.8 20.2 39 A THR CA 62 192.5 159.5 19.4 39 A THR CB 62 193.2 160.2 18.3 38 A THR OG1 62 194.2 159.4 17.6 37 A THR CG2 62 194.0 161.4 18.8 38 A THR C 62 191.5 158.5 18.8 39 A THR O 62 190.9 158.7 17.8 39 A TYR N 63 191.3 157.4 19.6 37 A TYR CA 63 190.3 156.4 19.2 35 A TYR CB 63 190.5 155.1 19.9 35 A TYR CG 63 189.4 154.0 19.8 35 A TYR CD1 63 189.4 153.1 18.7 35 A TYR CE1 63 188.4 152.2 18.6 34 A TYR CD2 63 188.3 154.0 20.6 34 A TYR CE2 63 187.2 153.1 20.5 34 A TYR CZ 63 187.3 152.2 19.4 34 A TYR OH 63 186.3 151.2 19.3 34 A TYR C 63 188.9 157.0 19.4 35 A TYR O 63 188.7 157.5 20.5 34 A VAL N 64 188.0 156.8 18.5 33 A VAL CA 64 186.7 157.3 18.6 32 A VAL CB 64 186.3 158.4 17.4 32 A VAL CG1 64 187.0 159.7 17.7 32 A VAL CG2 64 186.8 157.8 16.1 32 A VAL C 64 185.7 156.2 18.5 31 A VAL O 64 185.9 155.2 17.8 31 A LEU N 65 184.6 156.2 19.3 31 A LEU CA 65 183.6 155.2 19.4 30 A LEU CB 65 182.5 155.5 20.4 27 A LEU CG 65 183.0 155.7 21.8 26 A LEU CD1 65 181.9 156.2 22.7 26 A LEU CD2 65 183.5 154.5 22.4 27 A LEU C 65 182.9 155.1 18.0 32 A LEU O 65 182.8 156.1 17.3 33 A TYR N 66 182.6 153.9 17.6 34 A TYR CA 66 182.0 153.6 16.3 35 A TYR CB 66 181.5 152.2 16.1 34 A TYR CG 66 182.7 151.3 15.7 32 A TYR CD1 66 183.6 150.9 16.7 32 A TYR CE1 66 184.7 150.2 16.3 31 A TYR CD2 66 182.9 150.9 14.4 31 A TYR CE2 66 184.0 150.2 14.1 31 A TYR CZ 66 184.9 149.8 15.0 30 A TYR OH 66 186.0 149.1 14.6 29 A TYR C 66 180.8 154.5 15.9 36 A TYR O 66 180.5 154.8 14.7 35 A ARG N 67 180.0 154.9 16.9 38 A ARG CA 67 178.8 155.8 16.7 42 A ARG CB 67 177.9 155.7 17.9 42 A ARG CG 67 178.5 156.4 19.2 44 A ARG CD 67 177.5 156.6 20.2 45 A ARG NE 67 178.1 156.9 21.5 47 A ARG CZ 67 178.3 156.1 22.5 48 A ARG NH1 67 178.1 154.8 22.3 50 A ARG NH2 67 178.9 156.5 23.6 49 A ARG C 67 179.2 157.2 16.4 43 A ARG O 67 178.3 158.0 16.0 45 A ASP N 68 180.5 157.6 16.5 43 A ASP CA 68 180.9 158.9 16.2 42 A ASP CB 68 181.8 159.5 17.3 41 A ASP CG 68 181.1 159.6 18.6 40 A ASP OD1 68 179.9 160.0 18.7 39 A ASP OD2 68 181.8 159.4 19.7 39 A ASP C 68 181.7 158.9 14.9 43 A ASP O 68 182.3 159.9 14.5 44 A ARG N 69 181.6 157.8 14.2 44 A ARG CA 69 182.3 157.6 12.9 46 A ARG CB 69 183.0 156.2 12.9 46 A ARG CG 69 183.8 155.9 14.2 45 A ARG CD 69 185.0 154.9 14.0 44 A ARG NE 69 185.6 154.3 15.1 43 A ARG CZ 69 186.5 153.3 15.0 42 A ARG NH1 69 186.9 152.9 13.8 42 A ARG NH2 69 187.0 152.8 16.1 42 A ARG C 69 181.5 157.7 11.6 47 A ARG O 69 180.4 157.0 11.5 47 A ALA N 70 182.0 158.5 10.7 49 A ALA CA 70 181.3 158.8 9.4 50 A ALA CB 70 182.0 159.9 8.7 50 A ALA C 70 181.1 157.6 8.4 52 A ALA O 70 180.3 157.6 7.6 53 A GLU N 71 182.0 156.6 8.6 53 A GLU CA 71 181.9 155.4 7.7 54 A GLU CB 71 183.4 154.9 7.5 54 A GLU CG 71 184.2 154.5 8.7 55 A GLU CD 71 184.6 155.6 9.6 54 A GLU OE1 71 185.1 155.3 10.8 53 A GLU OE2 71 184.5 156.8 9.3 55 A GLU C 71 181.1 154.3 8.4 55 A GLU O 71 181.0 153.2 7.8 55 A TRP N 72 180.6 154.6 9.6 56 A TRP CA 72 179.8 153.7 10.4 58 A TRP CB 72 180.6 153.3 11.6 58 A TRP CG 72 181.6 152.2 11.4 57 A TRP CD2 72 181.3 150.8 11.1 57 A TRP CE2 72 182.5 150.2 10.9 57 A TRP CE3 72 180.1 150.1 10.9 57 A TRP CD1 72 182.9 152.3 11.4 57 A TRP NE1 72 183.5 151.1 11.1 57 A TRP CZ2 72 182.6 148.8 10.7 57 A TRP CZ3 72 180.2 148.7 10.7 57 A TRP CH2 72 181.5 148.1 10.5 57 A TRP C 72 178.5 154.4 10.8 59 A TRP O 72 177.8 153.9 11.8 59 A ALA N 73 178.0 155.4 10.1 60 A ALA CA 73 176.8 156.1 10.5 62 A ALA CB 73 176.9 157.6 10.4 62 A ALA C 73 175.6 155.6 9.6 62 A ALA O 73 174.4 155.9 9.8 62 A ASP N 74 176.0 154.8 8.5 62 A ASP CA 74 175.0 154.3 7.6 62 A ASP CB 74 175.6 154.0 6.3 62 A ASP CG 74 176.6 152.9 6.3 63 A ASP OD1 74 176.4 151.9 5.7 63 A ASP OD2 74 177.6 153.1 7.1 63 A ASP C 74 174.4 153.0 8.2 61 A ASP O 74 173.4 152.5 7.6 62 A ILE N 75 175.0 152.5 9.3 60 A ILE CA 75 174.5 151.3 9.9 60 A ILE CB 75 175.5 150.2 9.8 59 A ILE CG2 75 176.9 150.6 10.3 59 A ILE CG1 75 175.1 149.0 10.6 60 A ILE CD1 75 175.9 147.7 10.5 60 A ILE C 75 174.0 151.5 11.3 60 A ILE O 75 174.6 152.2 12.1 60 A ASP N 76 172.9 150.9 11.6 59 A ASP CA 76 172.2 150.9 12.9 59 A ASP CB 76 170.7 150.7 12.8 61 A ASP CG 76 169.9 151.9 12.8 63 A ASP OD1 76 169.8 152.7 11.8 64 A ASP OD2 76 169.2 152.2 13.9 63 A ASP C 76 172.8 149.9 13.9 58 A ASP O 76 172.8 148.7 13.6 57 A PRO N 77 173.4 150.3 15.0 56 A PRO CD 77 173.7 151.7 15.4 56 A PRO CA 77 173.9 149.4 15.9 56 A PRO CB 77 174.7 150.2 16.9 55 A PRO CG 77 173.9 151.5 16.9 56 A PRO C 77 172.8 148.6 16.6 55 A PRO O 77 171.7 149.1 16.8 55 A VAL N 78 173.1 147.3 17.0 54 A VAL CA 78 172.1 146.5 17.6 53 A VAL CB 78 172.0 145.2 16.8 53 A VAL CG1 78 170.9 144.3 17.5 53 A VAL CG2 78 171.6 145.4 15.4 52 A VAL C 78 172.5 146.2 19.1 53 A VAL O 78 173.5 145.4 19.3 53 A PRO N 79 171.9 146.8 20.0 53 A PRO CD 79 170.9 147.9 19.9 52 A PRO CA 79 172.2 146.5 21.4 52 A PRO CB 79 171.4 147.6 22.2 52 A PRO CG 79 170.2 147.8 21.3 52 A PRO C 79 171.9 145.1 21.9 52 A PRO O 79 170.9 144.5 21.4 51 A GLN N 80 172.7 144.6 22.7 52 A GLN CA 80 172.5 143.2 23.2 52 A GLN CB 80 173.6 142.8 24.2 51 A GLN CG 80 173.5 141.4 24.7 50 A GLN CD 80 174.7 140.9 25.5 50 A GLN OE1 80 175.7 140.3 24.9 50 A GLN NE2 80 174.7 141.3 26.7 50 A GLN C 80 171.2 143.0 24.0 52 A GLN O 80 170.8 143.8 24.8 53 A ASN N 81 170.4 142.0 23.7 52 A ASN CA 81 169.2 141.7 24.3 52 A ASN CB 81 168.2 141.1 23.3 53 A ASN CG 81 166.8 140.8 23.9 53 A ASN OD1 81 166.5 141.2 25.1 53 A ASN ND2 81 165.9 140.2 23.1 54 A ASN C 81 169.3 140.7 25.4 52 A ASN O 81 169.2 139.4 25.2 52 A ASP N 82 169.4 141.2 26.7 52 A ASP CA 82 169.5 140.3 27.8 53 A ASP CB 82 170.4 141.0 28.9 53 A ASP CG 82 171.8 140.8 28.8 53 A ASP OD1 82 172.2 140.0 27.8 53 A ASP OD2 82 172.6 141.4 29.5 53 A ASP C 82 168.1 140.0 28.4 53 A ASP O 82 168.0 139.3 29.4 53 A GLY N 83 167.1 140.6 27.7 54 A GLY CA 83 165.7 140.4 28.2 55 A GLY C 83 165.4 141.4 29.3 55 A GLY O 83 166.2 142.0 29.9 56 A PRO N 84 164.1 141.6 29.5 55 A PRO CD 84 162.9 140.8 29.0 55 A PRO CA 84 163.6 142.5 30.6 54 A PRO CB 84 162.1 142.3 30.6 55 A PRO CG 84 162.0 140.9 30.1 55 A PRO C 84 164.2 142.3 32.0 54 A PRO O 84 164.4 143.3 32.7 53 A SER N 85 164.5 141.1 32.3 53 A SER CA 85 165.0 140.8 33.7 52 A SER CB 85 164.0 140.1 34.5 53 A SER OG 85 162.9 140.9 34.8 54 A SER C 85 166.3 140.0 33.6 52 A SER O 85 166.3 138.8 33.9 51 A PRO N 86 167.4 140.6 33.3 51 A PRO CD 86 167.4 142.1 33.1 51 A PRO CA 86 168.8 140.1 33.2 50 A PRO CB 86 169.6 141.3 33.0 51 A PRO CG 86 168.7 142.3 32.3 51 A PRO C 86 169.3 139.3 34.4 48 A PRO O 86 168.7 139.5 35.5 48 A VAL N 87 170.2 138.4 34.2 46 A VAL CA 87 170.9 137.6 35.2 43 A VAL CB 87 170.4 136.2 35.3 43 A VAL CG1 87 169.6 136.0 36.6 43 A VAL CG2 87 169.6 135.8 34.1 42 A VAL C 87 172.4 137.7 34.8 41 A VAL O 87 172.7 137.9 33.6 40 A VAL N 88 173.3 137.4 35.7 39 A VAL CA 88 174.7 137.5 35.5 38 A VAL CB 88 175.4 136.1 35.2 37 A VAL CG1 88 175.4 135.3 36.5 37 A VAL CG2 88 174.7 135.4 34.1 37 A VAL C 88 175.0 138.4 34.3 39 A VAL O 88 175.6 138.0 33.3 39 A GLN N 89 174.5 139.7 34.5 39 A GLN CA 89 174.7 140.7 33.5 39 A GLN CB 89 173.5 141.7 33.7 40 A GLN CG 89 173.7 143.0 32.9 42 A GLN CD 89 172.5 144.0 33.1 43 A GLN OE1 89 172.2 144.3 34.3 43 A GLN NE2 89 171.8 144.3 32.1 44 A GLN C 89 176.0 141.5 33.7 39 A GLN O 89 176.4 141.8 34.8 40 A ILE N 90 176.6 141.8 32.6 38 A ILE CA 90 177.9 142.5 32.6 38 A ILE CB 90 178.9 141.8 31.7 37 A ILE CG2 90 180.3 142.4 31.9 38 A ILE CG1 90 179.0 140.3 31.9 37 A ILE CD1 90 179.5 139.5 30.8 35 A ILE C 90 177.8 144.0 32.3 38 A ILE O 90 177.3 144.4 31.2 39 A ILE N 91 178.2 144.8 33.2 37 A ILE CA 91 178.2 146.3 33.0 38 A ILE CB 91 178.4 147.0 34.4 38 A ILE CG2 91 178.2 148.5 34.1 38 A ILE CG1 91 177.4 146.6 35.4 38 A ILE CD1 91 175.9 146.7 35.0 38 A ILE C 91 179.4 146.7 32.1 37 A ILE O 91 180.4 147.1 32.5 37 A TYR N 92 179.1 146.5 30.8 36 A TYR CA 92 180.2 146.8 29.9 36 A TYR CB 92 179.8 146.4 28.4 36 A TYR CG 92 179.2 145.1 28.3 36 A TYR CD1 92 177.9 145.0 27.6 36 A TYR CE1 92 177.3 143.8 27.4 36 A TYR CD2 92 179.7 143.9 28.8 35 A TYR CE2 92 179.1 142.7 28.6 35 A TYR CZ 92 177.9 142.6 27.9 36 A TYR OH 92 177.2 141.4 27.8 35 A TYR C 92 180.7 148.2 29.9 37 A TYR O 92 180.0 149.1 30.2 37 A SER N 93 182.0 148.3 29.5 38 A SER CA 93 182.6 149.6 29.4 39 A SER CB 93 184.1 149.4 29.1 39 A SER OG 93 184.2 148.8 27.8 39 A SER C 93 181.9 150.2 28.2 40 A SER O 93 181.1 149.5 27.5 41 A GLU N 94 182.1 151.5 27.8 42 A GLU CA 94 181.4 152.0 26.7 43 A GLU CB 94 181.3 153.5 26.7 46 A GLU CG 94 180.4 154.1 25.7 49 A GLU CD 94 179.5 155.1 26.2 51 A GLU OE1 94 178.5 154.7 26.9 51 A GLU OE2 94 179.8 156.3 26.1 52 A GLU C 94 182.0 151.6 25.4 42 A GLU O 94 181.3 151.6 24.3 42 A LYS N 95 183.3 151.3 25.4 41 A LYS CA 95 184.0 150.9 24.1 41 A LYS CB 95 185.5 151.0 24.3 41 A LYS CG 95 186.1 152.4 24.4 43 A LYS CD 95 187.4 152.4 25.1 43 A LYS CE 95 188.5 151.7 24.2 43 A LYS NZ 95 189.7 151.4 25.0 43 A LYS C 95 183.6 149.5 23.8 40 A LYS O 95 183.2 149.1 22.7 40 A PHE N 96 183.6 148.6 24.9 39 A PHE CA 96 183.2 147.2 24.7 38 A PHE CB 96 183.2 146.5 26.1 37 A PHE CG 96 183.0 145.1 26.0 36 A PHE CD1 96 184.1 144.2 26.2 35 A PHE CD2 96 181.8 144.5 25.7 36 A PHE CE1 96 183.9 142.8 26.1 35 A PHE CE2 96 181.6 143.2 25.6 35 A PHE CZ 96 182.7 142.3 25.8 35 A PHE C 96 181.8 147.2 24.2 39 A PHE O 96 181.6 146.7 23.1 39 A ARG N 97 180.9 147.9 24.8 39 A ARG CA 97 179.6 148.0 24.4 39 A ARG CB 97 178.7 148.8 25.3 41 A ARG CG 97 177.3 148.4 25.4 45 A ARG CD 97 176.3 149.4 25.9 48 A ARG NE 97 176.8 150.2 27.0 50 A ARG CZ 97 177.3 151.5 26.9 52 A ARG NH1 97 177.4 152.1 25.7 53 A ARG NH2 97 177.8 152.1 28.0 53 A ARG C 97 179.5 148.6 23.0 38 A ARG O 97 178.7 148.1 22.1 39 A ASP N 98 180.2 149.6 22.7 37 A ASP CA 98 180.2 150.3 21.4 36 A ASP CB 98 181.1 151.5 21.4 37 A ASP CG 98 181.2 152.1 20.0 38 A ASP OD1 98 180.3 152.9 19.6 39 A ASP OD2 98 182.3 151.9 19.3 38 A ASP C 98 180.5 149.3 20.2 35 A ASP O 98 179.8 149.3 19.2 36 A VAL N 99 181.7 148.6 20.3 33 A VAL CA 99 182.1 147.7 19.3 31 A VAL CB 99 183.5 147.1 19.6 30 A VAL CG1 99 183.9 146.0 18.6 29 A VAL CG2 99 184.5 148.2 19.6 29 A VAL C 99 181.1 146.6 19.0 30 A VAL O 99 180.7 146.3 17.9 29 A TYR N 100 180.7 146.0 20.1 30 A TYR CA 100 179.7 144.9 20.0 30 A TYR CB 100 179.6 144.2 21.4 30 A TYR CG 100 180.8 143.2 21.5 30 A TYR CD1 100 181.8 143.5 22.3 30 A TYR CE1 100 182.9 142.6 22.3 30 A TYR CD2 100 180.8 142.1 20.6 30 A TYR CE2 100 181.9 141.2 20.7 30 A TYR CZ 100 182.9 141.5 21.5 29 A TYR OH 100 184.0 140.7 21.5 29 A TYR C 100 178.4 145.2 19.5 32 A TYR O 100 177.9 144.5 18.6 32 A ASP N 101 177.8 146.3 19.9 32 A ASP CA 101 176.5 146.8 19.4 33 A ASP CB 101 176.1 148.1 19.9 34 A ASP CG 101 175.4 148.0 21.3 36 A ASP OD1 101 175.3 146.9 21.8 36 A ASP OD2 101 174.9 149.0 21.8 38 A ASP C 101 176.7 146.8 17.9 33 A ASP O 101 175.8 146.5 17.1 32 A TYR N 102 177.8 147.3 17.4 34 A TYR CA 102 178.1 147.3 16.0 36 A TYR CB 102 179.2 148.3 15.7 37 A TYR CG 102 178.7 149.7 15.3 38 A TYR CD1 102 178.4 150.1 14.0 39 A TYR CE1 102 177.8 151.3 13.7 40 A TYR CD2 102 178.3 150.6 16.3 39 A TYR CE2 102 177.7 151.8 16.0 39 A TYR CZ 102 177.5 152.2 14.7 40 A TYR OH 102 176.8 153.4 14.4 40 A TYR C 102 178.4 146.0 15.4 35 A TYR O 102 178.0 145.7 14.2 35 A PHE N 103 179.0 145.1 16.1 36 A PHE CA 103 179.3 143.7 15.6 36 A PHE CB 103 180.1 142.9 16.6 35 A PHE CG 103 180.4 141.5 16.1 34 A PHE CD1 103 181.3 141.2 15.1 34 A PHE CD2 103 179.7 140.4 16.7 33 A PHE CE1 103 181.5 140.0 14.6 33 A PHE CE2 103 179.9 139.1 16.2 32 A PHE CZ 103 180.8 138.9 15.1 32 A PHE C 103 177.9 143.0 15.4 37 A PHE O 103 177.7 142.5 14.3 37 A ARG N 104 177.0 143.1 16.4 38 A ARG CA 104 175.7 142.4 16.2 38 A ARG CB 104 174.8 142.8 17.4 38 A ARG CG 104 175.4 142.3 18.7 38 A ARG CD 104 174.5 142.7 19.8 39 A ARG NE 104 175.1 142.3 21.1 41 A ARG CZ 104 175.9 143.1 21.8 42 A ARG NH1 104 176.3 144.3 21.3 42 A ARG NH2 104 176.5 142.7 22.9 42 A ARG C 104 175.1 143.0 14.9 38 A ARG O 104 174.5 142.2 14.2 38 A ALA N 105 175.2 144.3 14.7 38 A ALA CA 105 174.6 144.9 13.6 38 A ALA CB 105 175.0 146.4 13.6 39 A ALA C 105 175.2 144.3 12.3 39 A ALA O 105 174.4 143.9 11.5 39 A VAL N 106 176.5 144.2 12.2 39 A VAL CA 106 177.1 143.7 11.0 39 A VAL CB 106 178.7 144.0 11.0 39 A VAL CG1 106 179.5 142.9 10.3 40 A VAL CG2 106 178.9 145.3 10.4 39 A VAL C 106 176.9 142.2 10.8 39 A VAL O 106 176.6 141.7 9.7 38 A LEU N 107 176.9 141.4 11.9 40 A LEU CA 107 176.7 140.0 11.9 41 A LEU CB 107 176.9 139.4 13.3 39 A LEU CG 107 176.8 137.9 13.5 38 A LEU CD1 107 177.9 137.3 12.7 37 A LEU CD2 107 176.9 137.5 15.0 37 A LEU C 107 175.3 139.7 11.5 43 A LEU O 107 175.0 138.8 10.7 43 A GLN N 108 174.4 140.5 12.1 47 A GLN CA 108 172.9 140.4 11.8 49 A GLN CB 108 172.2 141.6 12.4 51 A GLN CG 108 170.9 141.4 13.1 52 A GLN CD 108 171.1 141.1 14.6 53 A GLN OE1 108 170.1 141.3 15.3 54 A GLN NE2 108 172.3 140.7 15.0 52 A GLN C 108 172.7 140.3 10.4 50 A GLN O 108 172.1 139.3 9.8 51 A ARG N 109 173.2 141.3 9.7 51 A ARG CA 109 173.0 141.4 8.2 52 A ARG CB 109 173.0 142.8 7.8 54 A ARG CG 109 174.2 143.6 8.1 56 A ARG CD 109 174.2 145.0 7.7 58 A ARG NE 109 173.1 145.8 8.4 60 A ARG CZ 109 172.5 146.9 7.9 61 A ARG NH1 109 172.8 147.3 6.6 62 A ARG NH2 109 171.6 147.5 8.6 61 A ARG C 109 174.0 140.6 7.5 51 A ARG O 109 174.0 140.5 6.3 51 A ASP N 110 174.9 139.9 8.2 50 A ASP CA 110 176.0 139.1 7.7 49 A ASP CB 110 175.5 137.8 7.1 49 A ASP CG 110 176.6 137.0 6.4 49 A ASP OD1 110 177.6 136.8 7.1 49 A ASP OD2 110 176.3 136.4 5.3 49 A ASP C 110 176.6 140.0 6.6 49 A ASP O 110 176.6 139.7 5.4 48 A GLU N 111 177.2 141.1 7.1 48 A GLU CA 111 177.8 142.1 6.2 48 A GLU CB 111 177.8 143.4 6.9 48 A GLU CG 111 178.0 144.6 6.0 47 A GLU CD 111 178.2 145.9 6.8 47 A GLU OE1 111 179.4 146.4 6.7 47 A GLU OE2 111 177.3 146.3 7.5 47 A GLU C 111 179.3 141.7 6.0 47 A GLU O 111 180.1 141.9 6.8 48 A ARG N 112 179.5 141.0 4.8 46 A ARG CA 112 180.9 140.6 4.5 45 A ARG CB 112 180.8 139.3 3.7 46 A ARG CG 112 180.2 138.2 4.4 47 A ARG CD 112 179.9 137.0 3.6 48 A ARG NE 112 179.0 136.1 4.5 50 A ARG CZ 112 178.8 134.8 4.2 51 A ARG NH1 112 179.3 134.2 3.2 51 A ARG NH2 112 178.0 134.2 5.1 52 A ARG C 112 181.8 141.6 3.9 45 A ARG O 112 182.3 141.4 2.8 44 A SER N 113 182.0 142.7 4.7 44 A SER CA 113 182.8 143.8 4.2 43 A SER CB 113 182.0 145.1 4.3 44 A SER OG 113 181.7 145.5 5.7 43 A SER C 113 184.1 144.0 5.0 42 A SER O 113 184.2 143.6 6.1 41 A GLU N 114 185.0 144.7 4.3 42 A GLU CA 114 186.3 145.1 4.8 42 A GLU CB 114 187.0 145.9 3.7 43 A GLU CG 114 188.3 146.4 4.1 45 A GLU CD 114 189.3 145.2 4.3 46 A GLU OE1 114 190.0 145.1 5.3 47 A GLU OE2 114 189.4 144.4 3.3 46 A GLU C 114 186.3 145.9 6.1 42 A GLU O 114 187.2 145.8 6.9 41 A ARG N 115 185.2 146.6 6.3 42 A ARG CA 115 185.0 147.4 7.6 42 A ARG CB 115 184.0 148.5 7.4 43 A ARG CG 115 182.6 148.1 7.0 44 A ARG CD 115 181.7 149.3 7.1 45 A ARG NE 115 180.3 149.0 6.7 46 A ARG CZ 115 179.2 149.7 7.0 46 A ARG NH1 115 178.0 149.3 6.6 46 A ARG NH2 115 179.3 150.7 7.8 46 A ARG C 115 184.6 146.4 8.7 42 A ARG O 115 185.0 146.5 9.8 42 A ALA N 116 183.7 145.5 8.3 42 A ALA CA 116 183.2 144.5 9.2 42 A ALA CB 116 182.3 143.5 8.6 41 A ALA C 116 184.5 143.7 9.7 41 A ALA O 116 184.7 143.5 10.9 41 A PHE N 117 185.3 143.4 8.7 40 A PHE CA 117 186.6 142.7 9.0 38 A PHE CB 117 187.3 142.5 7.7 38 A PHE CG 117 188.7 141.8 7.8 37 A PHE CD1 117 188.8 140.5 8.2 37 A PHE CD2 117 189.8 142.6 7.7 37 A PHE CE1 117 190.0 140.0 8.4 37 A PHE CE2 117 191.1 142.0 7.9 36 A PHE CZ 117 191.2 140.7 8.3 37 A PHE C 117 187.5 143.5 9.9 38 A PHE O 117 188.2 142.9 10.7 39 A LYS N 118 187.5 144.8 9.8 35 A LYS CA 118 188.4 145.5 10.8 32 A LYS CB 118 188.7 146.9 10.2 34 A LYS CG 118 189.6 146.9 8.9 36 A LYS CD 118 190.2 148.3 8.7 37 A LYS CE 118 190.9 148.4 7.3 38 A LYS NZ 118 190.0 148.2 6.1 39 A LYS C 118 187.8 145.7 12.1 30 A LYS O 118 188.5 145.8 13.1 30 A LEU N 119 186.4 145.6 12.2 28 A LEU CA 119 185.7 145.7 13.5 27 A LEU CB 119 184.2 146.0 13.2 26 A LEU CG 119 183.3 145.9 14.5 25 A LEU CD1 119 183.8 146.9 15.5 25 A LEU CD2 119 181.9 146.2 14.2 25 A LEU C 119 185.9 144.4 14.3 27 A LEU O 119 185.9 144.5 15.5 26 A THR N 120 185.9 143.3 13.6 27 A THR CA 120 186.1 142.0 14.3 26 A THR CB 120 186.1 140.8 13.4 26 A THR OG1 120 187.1 141.1 12.4 25 A THR CG2 120 184.8 140.6 12.8 27 A THR C 120 187.4 142.1 15.1 27 A THR O 120 187.5 141.6 16.2 28 A ARG N 121 188.4 142.7 14.5 28 A ARG CA 121 189.7 142.8 15.2 29 A ARG CB 121 190.7 143.5 14.4 30 A ARG CG 121 191.9 143.9 15.2 33 A ARG CD 121 192.7 145.0 14.6 36 A ARG NE 121 193.6 144.4 13.6 39 A ARG CZ 121 194.9 144.6 13.6 40 A ARG NH1 121 195.6 144.0 12.6 40 A ARG NH2 121 195.4 145.4 14.5 41 A ARG C 121 189.6 143.4 16.5 30 A ARG O 121 190.2 143.0 17.5 31 A ASP N 122 188.8 144.5 16.6 31 A ASP CA 122 188.5 145.2 17.9 30 A ASP CB 122 187.9 146.6 17.7 31 A ASP CG 122 188.8 147.6 17.1 32 A ASP OD1 122 190.0 147.7 17.5 32 A ASP OD2 122 188.3 148.4 16.2 32 A ASP C 122 187.7 144.4 18.8 30 A ASP O 122 187.8 144.4 20.0 30 A ALA N 123 186.7 143.8 18.2 30 A ALA CA 123 185.7 142.9 19.0 29 A ALA CB 123 184.6 142.4 18.1 29 A ALA C 123 186.6 141.8 19.6 29 A ALA O 123 186.4 141.4 20.7 30 A ILE N 124 187.6 141.3 18.8 27 A ILE CA 124 188.4 140.2 19.2 26 A ILE CB 124 189.3 139.7 18.1 25 A ILE CG2 124 190.6 139.2 18.6 25 A ILE CG1 124 188.5 138.7 17.3 24 A ILE CD1 124 189.2 138.1 16.1 24 A ILE C 124 189.3 140.8 20.4 26 A ILE O 124 189.5 140.2 21.4 26 A GLU N 125 189.9 141.9 20.1 27 A GLU CA 125 190.7 142.5 21.1 28 A GLU CB 125 191.2 143.9 20.7 32 A GLU CG 125 192.6 144.3 21.2 37 A GLU CD 125 193.1 145.6 20.6 41 A GLU OE1 125 193.7 146.5 21.3 42 A GLU OE2 125 192.9 145.8 19.3 42 A GLU C 125 190.0 142.7 22.5 27 A GLU O 125 190.5 142.4 23.5 25 A LEU N 126 188.7 143.1 22.4 25 A LEU CA 126 187.9 143.3 23.6 24 A LEU CB 126 186.7 144.1 23.2 22 A LEU CG 126 187.1 145.5 22.8 21 A LEU CD1 126 186.0 146.1 22.0 22 A LEU CD2 126 187.4 146.3 24.0 20 A LEU C 126 187.6 142.0 24.4 23 A LEU O 126 187.6 142.0 25.6 23 A ASN N 127 187.4 140.9 23.6 23 A ASN CA 127 187.2 139.6 24.3 23 A ASN CB 127 185.7 139.4 24.6 23 A ASN CG 127 185.5 138.1 25.4 23 A ASN OD1 127 186.5 137.6 25.9 25 A ASN ND2 127 184.3 137.6 25.5 23 A ASN C 127 187.6 138.5 23.3 22 A ASN O 127 186.8 137.9 22.6 22 A ALA N 128 188.9 138.3 23.3 21 A ALA CA 128 189.6 137.3 22.5 21 A ALA CB 128 191.1 137.3 22.7 20 A ALA C 128 189.0 135.9 22.6 20 A ALA O 128 189.3 135.1 21.8 22 A ALA N 129 188.1 135.7 23.6 18 A ALA CA 129 187.5 134.4 23.7 17 A ALA CB 129 187.4 134.1 25.2 17 A ALA C 129 186.1 134.3 23.1 18 A ALA O 129 185.4 133.3 23.2 17 A ASN N 130 185.7 135.4 22.4 18 A ASN CA 130 184.4 135.4 21.8 17 A ASN CB 130 183.9 136.8 21.5 19 A ASN CG 130 182.4 136.7 21.0 20 A ASN OD1 130 182.1 135.9 20.2 22 A ASN ND2 130 181.6 137.6 21.5 21 A ASN C 130 184.6 134.6 20.5 16 A ASN O 130 185.0 135.2 19.5 16 A TYR N 131 184.3 133.3 20.6 15 A TYR CA 131 184.4 132.4 19.5 15 A TYR CB 131 184.2 131.0 19.9 13 A TYR CG 131 182.9 130.7 20.5 13 A TYR CD1 131 181.8 130.3 19.7 13 A TYR CE1 131 180.5 130.1 20.3 12 A TYR CD2 131 182.6 130.9 21.9 13 A TYR CE2 131 181.3 130.8 22.4 13 A TYR CZ 131 180.3 130.4 21.6 12 A TYR OH 131 179.1 130.3 22.2 12 A TYR C 131 183.5 132.7 18.3 15 A TYR O 131 183.6 132.1 17.2 17 A THR N 132 182.4 133.4 18.5 15 A THR CA 132 181.5 133.7 17.5 15 A THR CB 132 180.2 134.4 18.0 15 A THR OG1 132 179.5 133.5 18.9 15 A THR CG2 132 179.3 134.6 16.8 16 A THR C 132 182.1 134.7 16.6 16 A THR O 132 181.8 134.8 15.4 16 A VAL N 133 182.9 135.6 17.1 17 A VAL CA 133 183.5 136.6 16.3 18 A VAL CB 133 184.1 137.8 17.2 18 A VAL CG1 133 184.6 138.9 16.3 18 A VAL CG2 133 183.0 138.3 18.1 18 A VAL C 133 184.6 136.0 15.5 20 A VAL O 133 184.7 136.3 14.3 22 A TRP N 134 185.4 135.1 16.1 20 A TRP CA 134 186.5 134.4 15.5 21 A TRP CB 134 187.2 133.5 16.4 19 A TRP CG 134 188.2 134.1 17.3 18 A TRP CD2 134 189.5 134.7 16.9 17 A TRP CE2 134 190.1 135.2 18.0 17 A TRP CE3 134 190.1 134.7 15.6 17 A TRP CD1 134 188.1 134.4 18.6 17 A TRP NE1 134 189.3 135.0 19.1 16 A TRP CZ2 134 191.4 135.7 17.9 17 A TRP CZ3 134 191.4 135.3 15.6 16 A TRP CH2 134 192.0 135.8 16.7 17 A TRP C 134 185.9 133.7 14.3 23 A TRP O 134 186.6 133.6 13.2 22 A HIS N 135 184.7 133.2 14.4 25 A HIS CA 135 184.1 132.4 13.3 28 A HIS CB 135 182.8 131.7 13.8 30 A HIS CG 135 182.0 131.1 12.7 32 A HIS CD2 135 181.1 131.6 11.9 33 A HIS ND1 135 182.3 129.8 12.3 33 A HIS CE1 135 181.5 129.6 11.2 34 A HIS NE2 135 180.8 130.7 11.0 34 A HIS C 135 183.7 133.4 12.2 29 A HIS O 135 184.1 133.1 11.0 29 A PHE N 136 183.0 134.5 12.5 29 A PHE CA 136 182.6 135.4 11.5 29 A PHE CB 136 181.8 136.6 12.1 31 A PHE CG 136 181.3 137.6 11.1 33 A PHE CD1 136 180.3 137.2 10.1 34 A PHE CD2 136 181.7 138.9 11.1 34 A PHE CE1 136 179.8 138.1 9.2 34 A PHE CE2 136 181.2 139.8 10.1 35 A PHE CZ 136 180.3 139.4 9.2 34 A PHE C 136 183.9 136.0 10.8 28 A PHE O 136 183.9 136.3 9.6 29 A ARG N 137 185.0 136.1 11.5 27 A ARG CA 137 186.2 136.6 10.9 25 A ARG CB 137 187.3 136.8 12.0 24 A ARG CG 137 188.5 137.4 11.5 23 A ARG CD 137 189.4 137.8 12.6 23 A ARG NE 137 190.7 138.2 12.1 23 A ARG CZ 137 191.1 139.5 11.9 22 A ARG NH1 137 190.2 140.5 12.2 22 A ARG NH2 137 192.3 139.8 11.5 22 A ARG C 137 186.8 135.6 9.9 25 A ARG O 137 187.2 136.0 8.8 25 A ARG N 138 186.8 134.3 10.2 25 A ARG CA 138 187.3 133.4 9.3 23 A ARG CB 138 187.2 132.0 9.8 22 A ARG CG 138 188.5 131.3 10.0 21 A ARG CD 138 188.9 131.2 11.4 20 A ARG NE 138 188.1 130.3 12.2 19 A ARG CZ 138 188.1 130.2 13.5 19 A ARG NH1 138 188.9 130.9 14.3 19 A ARG NH2 138 187.3 129.2 14.1 19 A ARG C 138 186.4 133.5 8.0 23 A ARG O 138 186.9 133.5 6.9 22 A VAL N 139 185.1 133.7 8.2 23 A VAL CA 139 184.2 133.9 7.1 24 A VAL CB 139 182.8 134.2 7.7 24 A VAL CG1 139 181.8 134.5 6.5 24 A VAL CG2 139 182.2 132.9 8.4 24 A VAL C 139 184.6 135.0 6.2 24 A VAL O 139 184.8 134.9 5.0 23 A LEU N 140 184.8 136.2 6.8 25 A LEU CA 140 185.3 137.4 6.1 26 A LEU CB 140 185.4 138.6 7.0 25 A LEU CG 140 183.9 139.0 7.4 25 A LEU CD1 140 184.0 140.1 8.4 25 A LEU CD2 140 183.2 139.3 6.2 24 A LEU C 140 186.6 137.1 5.4 28 A LEU O 140 186.8 137.4 4.2 29 A LEU N 141 187.5 136.4 6.1 29 A LEU CA 141 188.8 136.0 5.5 31 A LEU CB 141 189.6 135.2 6.5 29 A LEU CG 141 190.4 135.8 7.6 28 A LEU CD1 141 191.0 134.7 8.4 28 A LEU CD2 141 191.4 136.8 7.1 27 A LEU C 141 188.6 135.3 4.2 34 A LEU O 141 189.4 135.4 3.3 35 A ARG N 142 187.5 134.5 4.1 38 A ARG CA 142 187.3 133.7 2.9 41 A ARG CB 142 186.3 132.5 3.2 44 A ARG CG 142 186.6 131.8 4.5 48 A ARG CD 142 185.3 131.0 5.1 51 A ARG NE 142 185.3 130.8 6.5 53 A ARG CZ 142 184.9 129.8 7.2 54 A ARG NH1 142 184.4 128.7 6.6 56 A ARG NH2 142 184.8 129.8 8.6 54 A ARG C 142 186.7 134.6 1.8 41 A ARG O 142 187.2 134.7 0.7 40 A SER N 143 185.5 135.2 2.2 40 A SER CA 143 184.8 136.1 1.3 39 A SER CB 143 183.6 136.6 2.0 39 A SER OG 143 183.2 135.7 2.9 41 A SER C 143 185.6 137.2 0.7 39 A SER O 143 185.6 137.5 −0.5 39 A LEU N 144 186.4 137.9 1.5 38 A LEU CA 144 187.2 139.0 1.0 37 A LEU CB 144 187.4 140.1 2.2 37 A LEU CG 144 186.3 140.5 3.1 36 A LEU CD1 144 186.9 141.4 4.2 36 A LEU CD2 144 185.2 141.2 2.5 35 A LEU C 144 188.5 138.6 0.5 37 A LEU O 144 189.3 139.4 0.0 37 A GLN N 145 188.8 137.3 0.5 37 A GLN CA 145 190.1 136.7 0.0 38 A GLN CB 145 190.1 136.7 −1.5 40 A GLN CG 145 189.1 135.7 −2.0 44 A GLN CD 145 189.4 135.4 −3.5 46 A GLN OE1 145 189.3 136.3 −4.3 48 A GLN NE2 145 189.6 134.2 −3.8 48 A GLN C 145 191.2 137.5 0.6 36 A GLN O 145 192.0 138.1 −0.2 35 A LYS N 146 191.4 137.6 1.9 35 A LYS CA 146 192.4 138.3 2.5 34 A LYS CB 146 192.1 138.5 4.0 34 A LYS CG 146 190.7 139.2 4.3 35 A LYS CD 146 190.7 140.6 3.7 35 A LYS CE 146 191.8 141.4 4.2 35 A LYS NZ 146 191.6 142.8 3.7 35 A LYS C 146 193.7 137.6 2.4 35 A LYS O 146 193.7 136.3 2.3 34 A ASP N 147 194.8 138.3 2.5 34 A ASP CA 147 196.1 137.7 2.5 34 A ASP CB 147 197.2 138.8 2.3 34 A ASP CG 147 198.6 138.3 2.2 34 A ASP OD1 147 199.1 137.7 3.1 36 A ASP OD2 147 199.2 138.5 1.1 35 A ASP C 147 196.3 137.0 3.8 33 A ASP O 147 196.5 137.6 4.8 34 A LEU N 148 196.3 135.6 3.7 33 A LEU CA 148 196.5 134.8 4.9 32 A LEU CB 148 196.1 133.4 4.5 31 A LEU CG 148 194.6 133.2 4.1 31 A LEU CD1 148 194.3 131.7 3.7 31 A LEU CD2 148 193.7 133.6 5.2 31 A LEU C 148 197.9 134.9 5.5 31 A LEU O 148 198.1 134.6 6.7 31 A GLN N 149 198.9 135.3 4.7 32 A GLN CA 149 200.2 135.3 5.3 33 A GLN CB 149 201.2 135.5 4.2 34 A GLN CG 149 202.6 135.0 4.7 36 A GLN CD 149 202.4 133.6 5.4 37 A GLN OE1 149 202.2 132.6 4.8 38 A GLN NE2 149 202.5 133.7 6.7 39 A GLN C 149 200.2 136.5 6.2 34 A GLN O 149 201.1 136.6 7.0 35 A GLU N 150 199.4 137.5 5.9 36 A GLU CA 150 199.3 138.7 6.7 38 A GLU CB 150 198.7 139.9 6.0 41 A GLU CG 150 199.6 141.0 5.7 46 A GLU CD 150 200.9 140.6 4.8 49 A GLU OE1 150 202.0 141.0 5.2 51 A GLU OE2 150 200.7 140.1 3.7 50 A GLU C 150 198.5 138.4 8.0 37 A GLU O 150 198.9 138.8 9.1 37 A GLU N 151 197.5 137.6 7.8 34 A GLU CA 151 196.6 137.1 8.9 32 A GLU CB 151 195.4 136.4 8.4 31 A GLU CG 151 194.5 135.9 9.5 30 A GLU CD 151 193.7 137.0 10.2 30 A GLU OE1 151 193.5 138.1 9.7 30 A GLU OE2 151 193.3 136.7 11.4 30 A GLU C 151 197.5 136.3 9.8 31 A GLU O 151 197.3 136.3 11.0 31 A MET N 152 198.5 135.6 9.3 29 A MET CA 152 199.4 134.8 10.1 28 A MET CB 152 200.5 134.1 9.2 27 A MET CG 152 200.0 132.8 8.6 26 A MET SD 152 199.9 131.5 9.9 25 A MET CE 152 201.4 131.8 10.8 24 A MET C 152 200.1 135.8 11.0 28 A MET O 152 200.1 135.6 12.2 28 A ASN N 153 200.5 136.9 10.4 28 A ASN CA 153 201.2 137.9 11.2 28 A ASN CB 153 201.6 139.0 10.2 30 A ASN CG 153 202.6 138.6 9.2 30 A ASN OD1 153 202.9 137.4 9.2 31 A ASN ND2 153 203.0 139.5 8.3 30 A ASN C 153 200.3 138.5 12.3 28 A ASN O 153 200.8 138.7 13.4 27 A TYR N 154 199.0 138.6 12.1 27 A TYR CA 154 198.1 139.1 13.1 26 A TYR CB 154 196.7 139.2 12.4 25 A TYR CG 154 195.6 139.5 13.4 26 A TYR CD1 154 195.5 140.7 14.1 27 A TYR CE1 154 194.5 140.9 15.0 27 A TYR CD2 154 194.6 138.5 13.7 27 A TYR CE2 154 193.6 138.7 14.6 28 A TYR CZ 154 193.6 140.0 15.3 28 A TYR OH 154 192.6 140.1 16.3 30 A TYR C 154 198.0 138.1 14.2 25 A TYR O 154 198.3 138.4 15.4 26 A ILE N 155 197.7 136.9 13.8 24 A ILE CA 155 197.5 135.8 14.8 22 A ILE CB 155 197.0 134.5 14.2 21 A ILE CG2 155 198.1 133.7 13.6 21 A ILE CG1 155 196.2 133.7 15.2 21 A ILE CD1 155 195.0 134.4 15.7 21 A ILE C 155 198.8 135.6 15.6 21 A ILE O 155 198.8 135.2 16.8 21 A THR N 156 199.9 135.9 15.0 20 A THR CA 156 201.2 135.8 15.8 21 A THR CB 156 202.4 136.1 14.8 21 A THR OG1 156 202.3 135.2 13.7 22 A THR CG2 156 203.7 135.8 15.5 21 A THR C 156 201.2 136.8 16.9 21 A THR O 156 201.6 136.4 18.1 21 A ALA N 157 200.8 138.0 16.7 22 A ALA CA 157 200.8 139.1 17.7 22 A ALA CB 157 200.5 140.4 17.0 22 A ALA C 157 199.9 138.8 18.8 22 A ALA O 157 200.3 138.9 19.9 21 A ILE N 158 198.6 138.5 18.5 22 A ILE CA 158 197.6 138.3 19.5 22 A ILE CB 158 196.2 137.9 18.8 23 A ILE CG2 158 195.3 137.6 19.9 24 A ILE CG1 158 195.7 139.1 18.0 25 A ILE CD1 158 195.4 140.3 18.9 26 A ILE C 158 198.0 137.1 20.4 22 A ILE O 158 197.7 137.2 21.6 23 A ILE N 159 198.5 136.0 19.8 22 A ILE CA 159 198.9 134.9 20.6 21 A ILE CB 159 199.4 133.7 19.8 20 A ILE CG2 159 199.8 132.6 20.7 20 A ILE CG1 159 198.3 133.2 18.9 22 A ILE CD1 159 198.7 132.1 17.9 22 A ILE C 159 200.0 135.4 21.6 21 A ILE O 159 199.9 135.2 22.8 21 A GLU N 160 201.0 136.1 21.0 22 A GLU CA 160 202.1 136.5 21.8 23 A GLU CB 160 203.1 137.4 21.1 23 A GLU CG 160 203.9 136.6 20.0 22 A GLU CD 160 205.2 136.0 20.6 22 A GLU OE1 160 205.5 136.2 21.8 22 A GLU OE2 160 205.9 135.4 19.8 21 A GLU C 160 201.5 137.3 23.0 24 A GLU O 160 202.1 137.2 24.1 25 A GLU N 161 200.4 138.1 22.8 26 A GLU CA 161 199.9 138.8 24.0 28 A GLU CB 161 199.3 140.2 23.5 30 A GLU CG 161 198.2 140.1 22.5 33 A GLU CD 161 198.0 141.4 21.7 36 A GLU OE1 161 199.0 141.9 21.1 37 A GLU OE2 161 196.8 141.8 21.6 38 A GLU C 161 199.0 138.0 24.9 27 A GLU O 161 198.9 138.3 26.1 29 A GLN N 162 198.3 137.0 24.3 27 A GLN CA 162 197.4 136.1 25.1 26 A GLN CB 162 196.0 136.6 25.2 28 A GLN CG 162 195.3 137.2 23.9 31 A GLN CD 162 194.1 138.1 24.3 34 A GLN OE1 162 193.3 137.7 25.2 33 A GLN NE2 162 194.0 139.3 23.7 34 A GLN C 162 197.5 134.7 24.6 24 A GLN O 162 196.6 134.2 23.9 24 A PRO N 163 198.6 134.0 24.9 22 A PRO CD 163 199.6 134.4 25.9 21 A PRO CA 163 198.9 132.6 24.5 21 A PRO CB 163 200.4 132.5 24.8 20 A PRO CG 163 200.4 133.2 26.2 20 A PRO C 163 198.1 131.5 25.2 21 A PRO O 163 198.4 130.3 25.0 21 A LYS N 164 197.3 131.9 26.2 21 A LYS CA 164 196.5 131.0 27.0 20 A LYS CB 164 196.7 131.2 28.5 19 A LYS CG 164 198.0 130.7 28.9 20 A LYS CD 164 198.0 130.6 30.4 19 A LYS CE 164 199.4 130.2 30.8 20 A LYS NZ 164 199.3 130.0 32.3 21 A LYS C 164 195.0 131.2 26.6 20 A LYS O 164 194.2 131.6 27.4 22 A ASN N 165 194.7 130.9 25.3 20 A ASN CA 165 193.3 131.1 24.8 18 A ASN CB 165 193.2 132.5 24.2 17 A ASN CG 165 192.1 132.6 23.3 18 A ASN OD1 165 191.9 131.7 22.4 20 A ASN ND2 165 191.3 133.7 23.3 18 A ASN C 165 193.2 130.0 23.8 18 A ASN O 165 194.1 129.6 23.2 18 A TYR N 166 192.0 129.4 23.8 17 A TYR CA 166 191.7 128.3 22.8 17 A TYR CB 166 190.5 127.5 23.3 18 A TYR CG 166 190.7 126.6 24.5 20 A TYR CD1 166 190.6 127.1 25.8 21 A TYR CE1 166 190.8 126.3 26.9 22 A TYR CD2 166 191.0 125.3 24.3 22 A TYR CE2 166 191.2 124.4 25.4 23 A TYR CZ 166 191.0 124.9 26.7 22 A TYR OH 166 191.2 124.1 27.8 23 A TYR C 166 191.5 128.8 21.4 16 A TYR O 166 192.0 128.1 20.5 18 A GLN N 167 190.8 129.9 21.2 14 A GLN CA 167 190.5 130.4 19.9 12 A GLN CB 167 189.5 131.5 19.9 12 A GLN CG 167 188.1 131.1 20.3 12 A GLN CD 167 188.1 130.7 21.8 13 A GLN OE1 167 188.8 131.2 22.6 13 A GLN NE2 167 187.2 129.8 22.1 14 A GLN C 167 191.7 130.9 19.1 12 A GLN O 167 191.8 130.7 17.8 12 A VAL N 168 192.6 131.6 19.7 11 A VAL CA 168 193.8 132.2 19.1 11 A VAL CB 168 194.7 133.0 20.0 11 A VAL CG1 168 194.0 134.2 20.6 10 A VAL CG2 168 195.3 132.2 21.1 11 A VAL C 168 194.6 131.1 18.4 13 A VAL O 168 194.7 131.0 17.2 15 A TRP N 169 194.9 130.0 19.2 13 A TRP CA 169 195.6 128.9 18.6 11 A TRP CB 169 196.0 127.9 19.7 10 A TRP CG 169 197.0 128.5 20.6 10 A TRP CD2 169 198.4 128.5 20.4 11 A TRP CE2 169 199.0 129.1 21.6 11 A TRP CE3 169 199.3 128.1 19.4 11 A TRP CD1 169 196.8 129.1 21.9 10 A TRP NE1 169 198.0 129.4 22.4 11 A TRP CZ2 169 200.4 129.2 21.7 12 A TRP CZ3 169 200.6 128.2 19.5 11 A TRP CH2 169 201.2 128.8 20.6 12 A TRP C 169 194.9 128.2 17.6 12 A TRP O 169 195.4 128.0 16.5 12 A HIS N 170 193.6 127.9 17.8 13 A HIS CA 170 192.8 127.2 16.8 15 A HIS CB 170 191.4 126.9 17.2 17 A HIS CG 170 190.6 126.2 16.2 19 A HIS CD2 170 189.4 126.5 15.6 21 A HIS ND1 170 190.9 124.9 15.8 21 A HIS CE1 170 190.1 124.5 14.9 22 A HIS NE2 170 189.1 125.4 14.8 21 A HIS C 170 192.7 128.0 15.5 16 A HIS O 170 192.4 127.4 14.4 17 A HIS N 171 192.8 129.3 15.6 17 A HIS CA 171 192.7 130.2 14.5 17 A HIS CB 171 192.6 131.6 14.9 17 A HIS CG 171 192.3 132.5 13.8 17 A HIS CD2 171 193.0 133.6 13.3 18 A HIS ND1 171 191.2 132.4 13.0 17 A HIS CE1 171 191.2 133.4 12.1 17 A HIS NE2 171 192.3 134.1 12.2 18 A HIS C 171 194.0 130.0 13.7 18 A HIS O 171 194.0 129.8 12.5 18 A ARG N 172 195.1 129.9 14.5 18 A ARG CA 172 196.4 129.7 13.8 18 A ARG CB 172 197.5 129.7 14.9 17 A ARG CG 172 198.8 129.8 14.3 15 A ARG CD 172 199.9 130.2 15.2 15 A ARG NE 172 201.2 130.0 14.6 17 A ARG CZ 172 201.9 130.9 14.1 18 A ARG NH1 172 201.6 132.2 14.2 18 A ARG NH2 172 203.0 130.6 13.4 19 A ARG C 172 196.4 128.4 13.1 19 A ARG O 172 196.9 128.3 12.0 20 A ARG N 173 195.8 127.4 13.7 21 A ARG CA 173 195.8 126.0 13.1 22 A ARG CB 173 195.1 125.1 14.0 23 A ARG CG 173 194.8 123.7 13.3 25 A ARG CD 173 194.3 122.8 14.4 27 A ARG NE 173 193.8 121.6 13.7 30 A ARG CZ 173 194.0 120.4 14.2 31 A ARG NH1 173 194.7 120.1 15.2 32 A ARG NH2 173 193.5 119.3 13.5 32 A ARG C 173 195.0 126.1 11.8 21 A ARG O 173 195.4 125.4 10.8 22 A VAL N 174 193.9 126.8 11.8 22 A VAL CA 174 193.1 126.9 10.6 22 A VAL CB 174 191.8 127.6 10.8 20 A VAL CG1 174 191.1 127.9 9.6 19 A VAL CG2 174 191.0 126.8 11.8 20 A VAL C 174 193.9 127.6 9.4 24 A VAL O 174 193.8 127.2 8.3 26 A LEU N 175 194.6 128.7 9.7 24 A LEU CA 175 195.4 129.3 8.7 25 A LEU CB 175 196.1 130.6 9.3 25 A LEU CG 175 195.1 131.7 9.8 25 A LEU CD1 175 196.0 132.9 10.3 26 A LEU CD2 175 194.2 132.2 8.7 24 A LEU C 175 196.5 128.4 8.1 26 A LEU O 175 196.5 128.3 6.9 26 A VAL N 176 197.2 127.7 9.0 26 A VAL CA 176 198.3 126.8 8.5 26 A VAL CB 176 199.1 126.2 9.7 26 A VAL CG1 176 200.1 125.2 9.2 25 A VAL CG2 176 199.8 127.3 10.4 26 A VAL C 176 197.7 125.7 7.6 26 A VAL O 176 198.4 125.2 6.8 27 A GLU N 177 196.5 125.3 7.9 27 A GLU CA 177 195.8 124.3 7.1 28 A GLU CB 177 194.6 123.8 7.8 29 A GLU CG 177 194.9 123.0 9.0 30 A GLU CD 177 193.7 122.4 9.7 32 A GLU OE1 177 193.8 121.4 10.4 33 A GLU OE2 177 192.6 123.0 9.5 33 A GLU C 177 195.5 124.9 5.7 28 A GLU O 177 195.8 124.3 4.7 28 A TRP N 178 194.8 126.0 5.7 28 A TRP CA 178 194.4 126.7 4.5 28 A TRP CB 178 193.8 128.1 4.8 28 A TRP CG 178 192.4 128.1 5.2 27 A TRP CD2 178 191.7 129.2 5.8 27 A TRP CE2 178 190.4 128.8 6.0 26 A TRP CE3 178 192.1 130.5 6.2 27 A TRP CD1 178 191.5 127.2 5.0 27 A TRP NE1 178 190.3 127.6 5.5 26 A TRP CZ2 178 189.4 129.7 6.5 26 A TRP CZ3 178 191.2 131.3 6.8 26 A TRP CH2 178 189.8 130.9 7.0 26 A TRP C 178 195.7 126.9 3.6 29 A TRP O 178 195.6 126.7 2.4 30 A LEU N 179 196.7 127.4 4.3 29 A LEU CA 179 198.0 127.7 3.6 30 A LEU CB 179 198.8 128.6 4.5 30 A LEU CG 179 198.5 130.1 4.6 29 A LEU CD1 179 199.6 130.8 5.4 30 A LEU CD2 179 198.3 130.8 3.3 29 A LEU C 179 198.8 126.4 3.4 31 A LEU O 179 199.7 126.5 2.6 31 A LYS N 180 198.6 125.4 4.1 33 A LYS CA 180 199.4 124.2 4.0 34 A LYS CB 180 199.2 123.6 2.6 36 A LYS CG 180 197.8 123.3 2.2 39 A LYS CD 180 197.6 123.0 0.8 41 A LYS CE 180 196.1 122.5 0.5 42 A LYS NZ 180 195.8 121.2 1.3 43 A LYS C 180 200.9 124.5 4.2 34 A LYS O 180 201.8 123.9 3.7 35 A ASP N 181 201.1 125.6 5.1 32 A ASP CA 181 202.4 126.1 5.3 32 A ASP CB 181 202.5 127.5 4.9 32 A ASP CG 181 203.9 128.1 4.8 33 A ASP OD1 181 204.8 127.4 5.3 32 A ASP OD2 181 204.0 129.2 4.3 33 A ASP C 181 202.8 126.0 6.8 32 A ASP O 181 202.4 126.8 7.6 33 A PRO N 182 203.7 125.0 7.2 32 A PRO CD 182 203.9 123.8 6.4 31 A PRO CA 182 204.1 124.8 8.5 31 A PRO CB 182 204.3 123.3 8.6 31 A PRO CG 182 204.8 123.0 7.3 31 A PRO C 182 205.5 125.4 8.8 30 A PRO O 182 206.0 125.3 9.9 31 A SER N 183 206.1 126.0 7.7 30 A SER CA 183 207.4 126.6 7.8 31 A SER CB 183 207.7 127.4 6.6 32 A SER OG 183 207.0 128.7 6.7 34 A SER C 183 207.7 127.4 9.1 31 A SER O 183 208.8 127.2 9.6 32 A GLN N 184 206.8 128.3 9.5 30 A GLN CA 184 207.1 129.1 10.7 29 A GLN CB 184 206.7 130.6 10.4 31 A GLN CG 184 205.3 130.8 9.7 33 A GLN CD 184 205.0 132.2 9.4 34 A GLN OE1 184 205.3 133.1 10.1 35 A GLN NE2 184 204.3 132.4 8.3 33 A GLN C 184 206.7 128.7 12.1 28 A GLN O 184 207.1 129.3 13.1 27 A GLU N 185 205.9 127.6 12.1 26 A GLU CA 185 205.4 127.0 13.4 23 A GLU CB 185 204.5 125.8 13.2 22 A GLU CG 185 203.4 126.0 12.2 21 A GLU CD 185 202.6 127.3 12.5 21 A GLU OE1 185 201.8 127.4 13.4 20 A GLU OE2 185 202.9 128.3 11.7 22 A GLU C 185 206.4 126.6 14.5 22 A GLU O 185 206.4 127.1 15.6 22 A LEU N 186 207.4 125.7 14.2 22 A LEU CA 186 208.3 125.3 15.2 23 A LEU CB 186 209.2 124.2 14.7 22 A LEU CG 186 208.5 122.9 14.3 22 A LEU CD1 186 209.4 121.8 14.0 23 A LEU CD2 186 207.6 122.5 15.5 21 A LEU C 186 209.1 126.4 15.9 24 A LEU O 186 209.4 126.3 17.1 24 A GLU N 187 209.3 127.5 15.2 27 A GLU CA 187 210.0 128.7 15.7 28 A GLU CB 187 210.6 129.5 14.5 31 A GLU CG 187 211.5 130.6 14.9 34 A GLU CD 187 211.8 131.5 13.8 36 A GLU OE1 187 211.9 130.9 12.6 37 A GLU OE2 187 211.9 132.7 14.0 37 A GLU C 187 209.1 129.5 16.5 27 A GLU O 187 209.5 129.9 17.7 27 A PHE N 188 207.9 129.9 16.0 25 A PHE CA 188 207.0 130.7 16.7 23 A PHE CB 188 205.7 130.9 15.9 24 A PHE CG 188 204.5 131.3 16.7 25 A PHE CD1 188 204.5 132.6 17.3 25 A PHE CD2 188 203.5 130.5 16.8 25 A PHE CE1 188 203.5 133.0 18.1 25 A PHE CE2 188 202.4 130.9 17.6 25 A PHE CZ 188 202.4 132.1 18.2 25 A PHE C 188 206.6 130.0 18.0 22 A PHE O 188 206.6 130.7 19.1 21 A ILE N 189 206.3 128.8 18.0 21 A ILE CA 189 205.9 128.0 19.2 20 A ILE CB 189 205.6 126.5 18.8 18 A ILE CG2 189 205.1 125.8 20.1 18 A ILE CG1 189 204.5 126.4 17.8 17 A ILE CD1 189 204.1 125.1 17.4 16 A ILE C 189 207.0 128.0 20.2 20 A ILE O 189 206.8 128.1 21.4 19 A ALA N 190 208.3 127.9 19.7 21 A ALA CA 190 209.4 127.9 20.7 21 A ALA CB 190 210.7 127.5 20.0 21 A ALA C 190 209.6 129.3 21.3 21 A ALA O 190 210.2 129.4 22.3 21 A ASP N 191 209.1 130.4 20.6 22 A ASP CA 191 209.2 131.7 21.2 22 A ASP CB 191 209.0 132.8 20.3 24 A ASP CG 191 209.1 134.2 20.9 28 A ASP OD1 191 210.1 134.4 21.6 29 A ASP OD2 191 208.2 135.1 20.8 28 A ASP C 191 208.1 131.8 22.4 22 A ASP O 191 208.4 132.3 23.4 23 A ILE N 192 206.9 131.3 22.1 20 A ILE CA 192 205.9 131.3 23.1 18 A ILE CB 192 204.6 130.7 22.6 17 A ILE CG2 192 203.6 130.6 23.6 17 A ILE CG1 192 204.1 131.6 21.4 16 A ILE CD1 192 203.7 133.0 21.9 16 A ILE C 192 206.4 130.4 24.3 18 A ILE O 192 206.4 130.8 25.4 17 A LEU N 193 206.9 129.2 24.0 19 A LEU CA 193 207.4 128.3 25.0 21 A LEU CB 193 207.8 127.0 24.3 19 A LEU CG 193 206.7 126.1 23.9 19 A LEU CD1 193 207.3 124.8 23.5 19 A LEU CD2 193 205.8 125.9 25.1 20 A LEU C 193 208.6 128.9 25.7 22 A LEU O 193 209.0 128.4 26.7 23 A ASN N 194 209.2 129.9 25.1 23 A ASN CA 194 210.3 130.5 25.7 24 A ASN CB 194 211.2 131.3 24.7 27 A ASN CG 194 212.4 131.9 25.3 29 A ASN OD1 194 212.5 133.1 25.4 31 A ASN ND2 194 213.3 131.0 25.7 30 A ASN C 194 209.8 131.4 26.8 24 A ASN O 194 210.5 131.7 27.8 24 A GLN N 195 208.6 131.9 26.7 24 A GLN CA 195 208.0 132.8 27.6 23 A GLN CB 195 207.0 133.7 26.9 24 A GLN CG 195 207.7 134.6 25.9 25 A GLN CD 195 206.8 135.2 24.8 26 A GLN OE1 195 205.8 135.9 25.0 27 A GLN NE2 195 207.2 134.9 23.5 26 A GLN C 195 207.3 132.0 28.8 23 A GLN O 195 207.4 132.4 29.9 24 A ASP N 196 206.7 130.9 28.4 22 A ASP CA 196 206.1 130.0 29.4 20 A ASP CB 196 204.6 130.2 29.4 20 A ASP CG 196 203.8 129.3 30.3 21 A ASP OD1 196 204.4 128.3 30.8 21 A ASP OD2 196 202.6 129.5 30.4 22 A ASP C 196 206.3 128.6 28.8 19 A ASP O 196 205.7 128.1 27.9 18 A ALA N 197 207.3 127.9 29.4 18 A ALA CA 197 207.7 126.6 29.0 17 A ALA CB 197 209.0 126.2 29.6 17 A ALA C 197 206.7 125.4 29.1 17 A ALA O 197 206.9 124.3 28.7 17 A LYS N 198 205.5 125.8 29.7 16 A LYS CA 198 204.5 124.7 29.9 15 A LYS CB 198 204.4 124.5 31.4 15 A LYS CG 198 205.7 124.2 32.1 15 A LYS CD 198 205.6 123.8 33.6 16 A LYS CE 198 206.9 123.4 34.1 17 A LYS NZ 198 206.9 123.1 35.6 17 A LYS C 198 203.2 125.1 29.3 15 A LYS O 198 202.1 124.6 29.7 16 A ASN N 199 203.2 126.1 28.4 13 A ASN CA 199 201.9 126.5 27.8 14 A ASN CB 199 202.1 127.6 26.8 15 A ASN CG 199 200.9 128.3 26.4 16 A ASN OD1 199 200.0 127.8 25.7 17 A ASN ND2 199 200.7 129.5 26.9 18 A ASN C 199 201.3 125.3 27.1 15 A ASN O 199 201.7 124.8 26.1 19 A TYR N 200 200.3 124.7 27.8 14 A TYR CA 200 199.6 123.6 27.2 12 A TYR CB 200 198.3 123.3 28.1 14 A TYR CG 200 197.9 121.9 28.1 14 A TYR CD1 200 198.4 120.9 28.9 15 A TYR CE1 200 198.1 119.5 28.8 14 A TYR CD2 200 196.9 121.4 27.2 15 A TYR CE2 200 196.6 120.1 27.1 14 A TYR CZ 200 197.1 119.2 27.9 14 A TYR OH 200 196.7 117.9 27.7 14 A TYR C 200 199.1 123.7 25.8 12 A TYR O 200 199.3 122.9 25.0 12 A HIS N 201 198.6 124.9 25.5 12 A HIS CA 201 198.2 125.2 24.1 12 A HIS CB 201 197.5 126.6 24.0 13 A HIS CG 201 196.4 126.7 25.0 12 A HIS CD2 201 196.3 127.0 26.3 12 A HIS ND1 201 195.1 126.5 24.6 13 A HIS CE1 201 194.3 126.6 25.7 12 A HIS NE2 201 195.0 127.0 26.7 12 A HIS C 201 199.4 125.1 23.2 13 A HIS O 201 199.4 124.4 22.2 14 A ALA N 202 200.5 125.8 23.6 14 A ALA CA 202 201.7 125.8 22.8 14 A ALA CB 202 202.8 126.5 23.5 13 A ALA C 202 202.2 124.4 22.4 14 A ALA O 202 202.4 124.1 21.2 15 A TRP N 203 202.4 123.5 23.4 13 A TRP CA 203 202.8 122.1 23.2 12 A TRP CB 203 203.0 121.5 24.6 11 A TRP CG 203 204.2 121.9 25.2 10 A TRP CD2 203 205.6 121.5 24.8 10 A TRP CE2 203 206.4 122.1 25.8  9 A TRP CE3 203 206.1 120.8 23.8  9 A TRP CD1 203 204.3 122.6 26.4  9 A TRP NE1 203 205.7 122.7 26.7 10 A TRP CZ2 203 207.8 122.0 25.7  9 A TRP CZ3 203 207.5 120.7 23.7  9 A TRP CH2 203 208.3 121.2 24.7  9 A TRP C 203 201.8 121.3 22.4 14 A TRP O 203 202.2 120.6 21.5 15 A GLN N 204 200.5 121.5 22.7 15 A GLN CA 204 199.5 120.7 21.9 15 A GLN CB 204 198.1 121.0 22.5 15 A GLN CG 204 197.1 120.1 21.8 15 A GLN CD 204 195.6 120.4 22.3 15 A GLN OE1 204 194.7 120.4 21.4 15 A GLN NE2 204 195.4 120.6 23.6 15 A GLN C 204 199.5 121.1 20.5 15 A GLN O 204 199.3 120.3 19.6 15 A HIS N 205 199.8 122.4 20.2 16 A HIS CA 205 199.8 122.9 18.8 18 A HIS CB 205 199.9 124.4 18.8 19 A HIS CG 205 199.9 125.0 17.4 20 A HIS CD2 205 200.7 125.9 16.8 20 A HIS ND1 205 198.9 124.7 16.5 21 A HIS CE1 205 199.1 125.3 15.4 20 A HIS NE2 205 200.2 126.1 15.5 20 A HIS C 205 201.1 122.3 18.2 19 A HIS O 205 201.0 121.8 17.1 20 A ARG N 206 202.2 122.4 19.0 19 A ARG CA 206 203.5 121.9 18.6 17 A ARG CB 206 204.5 122.0 19.7 16 A ARG CG 206 205.9 121.8 19.2 15 A ARG CD 206 206.9 122.2 20.3 16 A ARG NE 206 208.3 122.2 19.8 17 A ARG CZ 206 208.9 123.2 19.2 19 A ARG NH1 206 208.3 124.3 19.0 20 A ARG NH2 206 210.1 123.1 18.7 19 A ARG C 206 203.3 120.5 18.1 17 A ARG O 206 203.7 120.1 17.0 19 A GLN N 207 202.7 119.6 18.9 16 A GLN CA 207 202.5 118.2 18.6 17 A GLN CB 207 201.8 117.4 19.7 17 A GLN CG 207 202.8 117.2 20.9 17 A GLN CD 207 202.2 116.2 22.0 17 A GLN OE1 207 201.0 115.8 21.9 17 A GLN NE2 207 203.0 115.9 23.0 15 A GLN C 207 201.7 118.0 17.2 17 A GLN O 207 202.1 117.2 16.4 18 A TRP N 208 200.7 118.8 17.0 18 A TRP CA 208 199.9 118.6 15.8 18 A TRP CB 208 198.6 119.4 15.9 16 A TRP CG 208 197.9 119.6 14.6 15 A TRP CD2 208 198.1 120.8 13.7 15 A TRP CE2 208 197.3 120.6 12.6 15 A TRP CE3 208 198.9 121.9 13.8 16 A TRP CD1 208 197.0 118.8 14.0 15 A TRP NE1 208 196.7 119.4 12.8 15 A TRP CZ2 208 197.2 121.5 11.5 15 A TRP CZ3 208 198.8 122.8 12.8 16 A TRP CH2 208 198.0 122.6 11.6 15 A TRP C 208 200.7 119.1 14.6 20 A TRP O 208 200.4 118.5 13.5 21 A VAL N 209 201.5 120.1 14.7 20 A VAL CA 209 202.3 120.5 13.5 21 A VAL CB 209 203.0 121.8 13.7 21 A VAL CG1 209 203.8 122.2 12.5 21 A VAL CG2 209 202.1 122.9 14.1 22 A VAL C 209 203.3 119.4 13.2 22 A VAL O 209 203.5 119.1 12.0 23 A ILE N 210 204.0 118.9 14.2 22 A ILE CA 210 205.0 117.8 14.0 21 A ILE CB 210 205.7 117.4 15.3 19 A ILE CG2 210 206.5 116.2 15.1 18 A ILE CG1 210 206.5 118.6 15.8 17 A ILE CD1 210 207.3 118.2 17.0 15 A ILE C 210 204.3 116.6 13.4 24 A ILE O 210 204.8 116.0 12.5 25 A GLN N 211 203.2 116.2 14.0 28 A GLN CA 211 202.5 115.0 13.5 32 A GLN CB 211 201.4 114.6 14.5 34 A GLN CG 211 200.8 113.2 14.3 37 A GLN CD 211 200.5 112.4 15.6 39 A GLN OE1 211 200.0 113.0 16.6 40 A GLN NE2 211 200.7 111.1 15.6 39 A GLN C 211 202.0 115.1 12.1 33 A GLN O 211 202.2 114.3 11.3 34 A GLU N 212 201.4 116.3 11.8 36 A GLU CA 212 200.8 116.5 10.5 38 A GLU CB 212 200.0 117.8 10.5 40 A GLU CG 212 198.7 117.7 11.2 44 A GLU CD 212 197.9 116.5 10.5 46 A GLU OE1 212 197.6 116.7 9.3 48 A GLU OE2 212 197.6 115.5 11.2 47 A GLU C 212 201.8 116.6 9.4 38 A GLU O 212 201.7 115.9 8.4 38 A PHE N 213 202.8 117.5 9.5 37 A PHE CA 213 203.8 117.7 8.5 36 A PHE CB 213 204.1 119.2 8.4 35 A PHE CG 213 202.9 120.0 8.2 33 A PHE CD1 213 202.1 120.3 9.2 33 A PHE CD2 213 202.7 120.5 6.9 33 A PHE CE1 213 200.9 121.0 9.0 33 A PHE CE2 213 201.5 121.2 6.7 32 A PHE CZ 213 200.6 121.5 7.7 32 A PHE C 213 205.1 116.8 8.7 37 A PHE O 213 206.1 117.1 8.0 38 A ARG N 214 205.0 115.8 9.5 38 A ARG CA 214 206.1 114.9 9.7 39 A ARG CB 214 206.3 114.1 8.5 42 A ARG CG 214 205.3 112.9 8.4 46 A ARG CD 214 204.8 112.7 7.0 50 A ARG NE 214 203.3 113.0 6.9 54 A ARG CZ 214 202.4 112.2 7.4 56 A ARG NH1 214 201.1 112.6 7.3 57 A ARG NH2 214 202.7 111.1 8.0 57 A ARG C 214 207.4 115.6 10.0 38 A ARG O 214 208.5 115.2 9.6 39 A LEU N 215 207.3 116.7 10.9 35 A LEU CA 215 208.5 117.4 11.3 33 A LEU CB 215 208.2 118.9 11.4 32 A LEU CG 215 207.3 119.5 10.3 32 A LEU CD1 215 206.9 120.9 10.7 32 A LEU CD2 215 208.1 119.4 9.0 32 A LEU C 215 209.2 116.9 12.5 32 A LEU O 215 209.4 117.6 13.5 32 A TRP N 216 209.6 115.6 12.5 32 A TRP CA 216 210.2 114.9 13.6 31 A TRP CB 216 209.9 113.4 13.6 28 A TRP CG 216 208.5 113.0 13.5 25 A TRP CD2 216 207.5 112.9 14.5 24 A TRP CE2 216 206.3 112.6 13.9 24 A TRP CE3 216 207.6 113.1 15.9 23 A TRP CD1 216 207.8 112.8 12.3 25 A TRP NE1 216 206.5 112.5 12.6 24 A TRP CZ2 216 205.1 112.4 14.7 24 A TRP CZ3 216 206.5 112.9 16.7 23 A TRP CH2 216 205.2 112.6 16.1 23 A TRP C 216 211.7 115.2 13.9 33 A TRP O 216 212.1 115.4 15.0 34 A ASP N 217 212.5 115.1 12.8 35 A ASP CA 217 213.9 115.2 12.8 37 A ASP CB 217 214.4 115.7 11.5 39 A ASP CG 217 214.0 114.8 10.3 41 A ASP OD1 217 214.4 115.1 9.2 42 A ASP OD2 217 213.2 113.8 10.6 41 A ASP C 217 214.6 115.9 13.9 36 A ASP O 217 215.6 115.4 14.5 36 A ASN N 218 214.2 117.1 14.2 37 A ASN CA 218 214.9 117.9 15.3 37 A ASN CB 218 215.3 119.2 14.7 38 A ASN CG 218 215.9 119.1 13.3 39 A ASN OD1 218 215.2 119.3 12.3 40 A ASN ND2 218 217.2 118.8 13.3 39 A ASN C 218 214.1 118.1 16.6 36 A ASN O 218 214.6 118.9 17.4 37 A GLU N 219 213.0 117.4 16.8 34 A GLU CA 219 212.3 117.6 18.0 33 A GLU CB 219 210.8 117.1 17.9 33 A GLU CG 219 209.9 117.6 19.0 32 A GLU CD 219 209.8 119.1 19.2 32 A GLU OE1 219 210.5 119.9 18.4 32 A GLU OE2 219 209.1 119.6 20.1 32 A GLU C 219 212.9 117.0 19.3 33 A GLU O 219 212.8 117.6 20.4 33 A LEU N 220 213.6 115.9 19.2 32 A LEU CA 220 214.2 115.3 20.3 32 A LEU CB 220 214.7 113.8 20.1 32 A LEU CG 220 215.3 113.0 21.2 31 A LEU CD1 220 214.5 113.2 22.5 32 A LEU CD2 220 215.5 111.6 20.9 31 A LEU C 220 215.4 116.2 20.8 33 A LEU O 220 215.7 116.2 22.0 34 A GLN N 221 216.0 116.9 19.9 34 A GLN CA 221 217.1 117.8 20.2 36 A GLN CB 221 217.7 118.3 18.9 39 A GLN CG 221 218.8 119.4 19.1 42 A GLN CD 221 219.5 119.7 17.8 45 A GLN OE1 221 220.0 118.8 17.1 46 A GLN NE2 221 219.5 121.0 17.5 46 A GLN C 221 216.6 119.0 21.0 35 A GLN O 221 217.2 119.4 21.9 35 A TYR N 222 215.4 119.5 20.6 34 A TYR CA 222 214.8 120.6 21.2 33 A TYR CB 222 213.5 120.9 20.5 31 A TYR CG 222 212.7 122.1 21.0 31 A TYR CD1 222 213.3 123.3 21.2 30 A TYR CE1 222 212.6 124.4 21.7 30 A TYR CD2 222 211.4 121.9 21.4 30 A TYR CE2 222 210.7 123.0 21.9 29 A TYR CZ 222 211.3 124.2 22.1 30 A TYR OH 222 210.6 125.3 22.6 29 A TYR C 222 214.4 120.1 22.7 33 A TYR O 222 214.5 120.9 23.6 32 A VAL N 223 213.9 118.9 22.8 33 A VAL CA 223 213.6 118.3 24.1 32 A VAL CB 223 212.9 116.9 23.9 31 A VAL CG1 223 213.0 116.1 25.2 31 A VAL CG2 223 211.5 117.1 23.5 30 A VAL C 223 214.8 118.3 25.0 33 A VAL O 223 214.7 118.7 26.2 33 A ASP N 224 215.9 117.9 24.5 33 A ASP CA 224 217.1 117.8 25.4 35 A ASP CB 224 218.3 117.2 24.6 35 A ASP CG 224 218.1 115.8 24.3 36 A ASP OD1 224 217.6 115.0 25.1 36 A ASP OD2 224 218.4 115.5 23.1 36 A ASP C 224 217.4 119.3 25.8 35 A ASP O 224 217.9 119.5 26.9 35 A GLN N 225 217.2 120.2 24.9 35 A GLN CA 225 217.4 121.6 25.2 36 A GLN CB 225 217.1 122.5 24.0 37 A GLN CG 225 217.3 124.0 24.2 40 A GLN CD 225 216.7 124.9 23.1 42 A GLN OE1 225 216.7 124.5 21.9 42 A GLN NE2 225 216.3 126.1 23.4 42 A GLN C 225 216.6 122.0 26.4 35 A GLN O 225 217.2 122.4 27.4 35 A LEU N 226 215.3 121.9 26.3 34 A LEU CA 226 214.4 122.3 27.4 32 A LEU CB 226 213.0 122.3 27.0 31 A LEU CG 226 212.7 123.2 25.8 30 A LEU CD1 226 211.2 123.3 25.6 31 A LEU CD2 226 213.2 124.6 26.0 30 A LEU C 226 214.6 121.6 28.7 32 A LEU O 226 214.6 122.1 29.8 32 A LEU N 227 214.9 120.3 28.6 33 A LEU CA 227 215.2 119.4 29.8 33 A LEU CB 227 215.3 117.9 29.4 31 A LEU CG 227 214.1 117.1 29.3 30 A LEU CD1 227 214.5 115.7 28.8 30 A LEU CD2 227 213.3 117.1 30.6 29 A LEU C 227 216.4 119.9 30.5 34 A LEU O 227 216.5 119.7 31.8 33 A LYS N 228 217.4 120.4 29.8 35 A LYS CA 228 218.6 121.0 30.3 36 A LYS CB 228 219.6 121.3 29.2 38 A LYS CG 228 220.9 121.7 29.6 42 A LYS CD 228 221.8 121.7 28.4 45 A LYS CE 228 223.3 121.9 28.7 47 A LYS NZ 228 224.1 121.6 27.5 48 A LYS C 228 218.2 122.2 31.0 36 A LYS O 228 218.7 122.5 32.2 36 A GLU N 229 217.4 123.0 30.4 35 A GLU CA 229 216.9 124.3 31.0 33 A GLU CB 229 216.1 125.1 30.0 33 A GLU CG 229 216.9 125.4 28.7 33 A GLU CD 229 216.2 126.4 27.8 34 A GLU OE1 229 215.2 127.0 28.2 35 A GLU OE2 229 216.7 126.6 26.7 34 A GLU C 229 216.1 124.0 32.3 32 A GLU O 229 216.3 124.7 33.3 32 A ASP N 230 215.3 123.0 32.2 31 A ASP CA 230 214.5 122.6 33.4 31 A ASP CB 230 213.3 123.5 33.5 30 A ASP CG 230 212.6 123.3 34.9 30 A ASP OD1 230 213.0 122.5 35.7 30 A ASP OD2 230 211.6 124.0 35.1 29 A ASP C 230 214.1 121.1 33.4 30 A ASP O 230 213.1 120.7 32.8 30 A VAL N 231 215.0 120.3 34.0 30 A VAL CA 231 214.7 118.8 34.1 30 A VAL CB 231 215.8 118.1 34.8 30 A VAL CG1 231 215.8 118.3 36.3 29 A VAL CG2 231 215.7 116.6 34.5 30 A VAL C 231 213.3 118.5 34.7 30 A VAL O 231 212.8 117.4 34.6 30 A ARG N 232 212.8 119.5 35.5 29 A ARG CA 232 211.5 119.2 36.1 28 A ARG CB 232 211.5 120.1 37.4 27 A ARG CG 232 212.6 119.8 38.4 28 A ARG CD 232 212.2 120.5 39.7 29 A ARG NE 232 213.2 120.2 40.8 30 A ARG CZ 232 214.3 120.8 41.0 30 A ARG NH1 232 214.7 121.7 40.2 30 A ARG NH2 232 215.1 120.5 42.1 30 A ARG C 232 210.3 119.6 35.2 27 A ARG O 232 209.2 119.6 35.7 27 A ASN N 233 210.6 120.0 34.0 25 A ASN CA 233 209.5 120.3 33.1 24 A ASN CB 233 210.0 121.2 31.9 24 A ASN CG 233 208.8 121.7 31.1 24 A ASN OD1 233 207.7 121.2 31.1 25 A ASN ND2 233 209.1 122.8 30.4 23 A ASN C 233 208.8 119.1 32.6 24 A ASN O 233 209.1 118.5 31.6 25 A ASN N 234 207.7 118.8 33.3 24 A ASN CA 234 206.9 117.6 32.8 23 A ASN CB 234 205.7 117.4 33.8 23 A ASN CG 234 205.4 115.9 33.9 23 A ASN OD1 234 206.1 115.2 34.7 23 A ASN ND2 234 204.4 115.4 33.3 24 A ASN C 234 206.4 117.7 31.4 23 A ASN O 234 206.3 116.6 30.7 23 A SER N 235 206.2 118.8 30.9 21 A SER CA 235 205.7 119.0 29.5 20 A SER CB 235 205.3 120.4 29.2 20 A SER OG 235 204.2 120.8 30.0 21 A SER C 235 206.8 118.5 28.5 20 A SER O 235 206.5 117.9 27.4 19 A VAL N 236 208.1 118.7 28.9 19 A VAL CA 236 209.2 118.3 28.0 18 A VAL CB 236 210.4 118.9 28.4 18 A VAL CG1 236 211.5 118.6 27.4 19 A VAL CG2 236 210.2 120.4 28.5 18 A VAL C 236 209.3 116.8 28.1 18 A VAL O 236 209.5 116.1 27.0 18 A TRP N 237 209.2 116.2 29.3 18 A TRP CA 237 209.3 114.7 29.4 19 A TRP CB 237 209.2 114.3 30.9 19 A TRP CG 237 210.4 114.5 31.7 20 A TRP CD2 237 211.6 113.6 31.7 21 A TRP CE2 237 212.5 114.2 32.5 21 A TRP CE3 237 211.9 112.5 31.0 21 A TRP CD1 237 210.7 115.5 32.5 21 A TRP NE1 237 211.9 115.4 33.0 21 A TRP CZ2 237 213.8 113.7 32.8 20 A TRP CZ3 237 213.2 111.9 31.3 21 A TRP CH2 237 214.1 112.5 32.1 21 A TRP C 237 208.1 114.2 28.6 19 A TRP O 237 208.3 113.2 27.9 20 A ASN N 238 207.0 114.8 28.7 19 A ASN CA 238 205.9 114.3 27.9 20 A ASN CB 238 204.6 115.0 28.2 21 A ASN CG 238 203.5 114.5 27.3 22 A ASN OD1 238 203.2 113.3 27.3 23 A ASN ND2 238 203.0 115.4 26.4 23 A ASN C 238 206.2 114.4 26.4 19 A ASN O 238 206.0 113.4 25.7 19 A GLN N 239 206.9 115.5 26.0 20 A GLN CA 239 207.2 115.7 24.6 21 A GLN CB 239 207.8 117.1 24.3 20 A GLN CG 239 208.1 117.4 22.9 19 A GLN CD 239 206.8 117.7 22.0 19 A GLN OE1 239 205.7 117.4 22.5 19 A GLN NE2 239 207.0 118.2 20.9 18 A GLN C 239 208.2 114.7 24.1 22 A GLN O 239 208.2 114.3 22.9 22 A ARG N 240 209.1 114.3 25.0 23 A ARG CA 240 210.2 113.3 24.7 23 A ARG CB 240 211.0 113.1 26.0 23 A ARG CG 240 212.2 112.3 25.8 23 A ARG CD 240 213.0 112.2 27.1 24 A ARG NE 240 214.3 111.6 26.7 25 A ARG CZ 240 215.4 112.2 26.2 26 A ARG NH1 240 215.3 113.6 26.1 27 A ARG NH2 240 216.3 111.6 25.7 27 A ARG C 240 209.5 112.0 24.4 23 A ARG O 240 209.7 111.4 23.3 26 A HIS N 241 208.6 111.5 25.2 22 A HIS CA 241 207.9 110.3 25.0 22 A HIS CB 241 206.9 110.1 26.1 23 A HIS CG 241 206.3 108.7 26.1 24 A HIS CD2 241 206.6 107.6 26.9 24 A HIS ND1 241 205.3 108.3 25.3 24 A HIS CE1 241 204.9 107.1 25.5 24 A HIS NE2 241 205.7 106.6 26.5 25 A HIS C 241 207.1 110.4 23.6 22 A HIS O 241 207.1 109.4 22.9 23 A PHE N 242 206.5 111.5 23.3 21 A PHE CA 242 205.7 111.6 22.1 20 A PHE CB 242 205.0 113.0 22.1 20 A PHE CG 242 204.3 113.4 20.8 19 A PHE CD1 242 203.1 112.9 20.4 19 A PHE CD2 242 204.9 114.3 19.9 19 A PHE CE1 242 202.4 113.3 19.3 18 A PHE CE2 242 204.3 114.7 18.7 19 A PHE CZ 242 203.0 114.2 18.4 18 A PHE C 242 206.6 111.5 20.9 21 A PHE O 242 206.3 110.8 19.9 21 A VAL N 243 207.8 112.1 21.0 21 A VAL CA 243 208.8 112.0 19.9 22 A VAL CB 243 210.0 113.0 20.2 22 A VAL CG1 243 211.1 112.7 19.3 22 A VAL CG2 243 209.5 114.4 20.0 23 A VAL C 243 209.3 110.6 19.6 22 A VAL O 243 209.3 110.1 18.5 22 A ILE N 244 209.8 109.9 20.7 22 A ILE CA 244 210.4 108.6 20.6 22 A ILE CB 244 211.0 108.2 21.9 21 A ILE CG2 244 211.6 106.8 21.8 22 A ILE CG1 244 212.1 109.2 22.3 19 A ILE CD1 244 212.7 108.8 23.6 18 A ILE C 244 209.2 107.6 20.2 22 A ILE O 244 209.3 106.9 19.3 21 A SER N 245 208.1 107.7 20.9 24 A SER CA 245 207.0 106.9 20.6 26 A SER CB 245 205.8 107.4 21.3 27 A SER OG 245 205.9 107.1 22.7 30 A SER C 245 206.6 106.9 19.1 29 A SER O 245 206.2 105.9 18.6 30 A ASN N 246 206.6 108.1 18.5 31 A ASN CA 246 206.2 108.1 17.1 31 A ASN CB 246 205.4 109.4 16.8 31 A ASN CG 246 204.1 109.4 17.6 31 A ASN OD1 246 204.0 109.7 18.8 31 A ASN ND2 246 203.0 109.1 16.9 32 A ASN C 246 207.3 108.0 16.1 32 A ASN O 246 207.2 108.1 14.9 32 A THR N 247 208.5 107.8 16.6 32 A THR CA 247 209.7 107.6 15.7 33 A THR CB 247 210.7 108.8 15.9 32 A THR OG1 247 211.1 108.8 17.3 32 A THR CG2 247 210.1 110.1 15.6 31 A THR C 247 210.3 106.2 15.8 34 A THR O 247 209.9 105.3 15.0 34 A THR N 248 211.1 106.0 16.8 34 A THR CA 248 211.7 104.7 17.0 35 A THR CB 248 213.1 104.9 17.6 34 A THR OG1 248 213.1 105.4 18.9 34 A THR CG2 248 213.8 106.0 16.7 34 A THR C 248 211.0 103.7 18.0 36 A THR O 248 211.3 102.5 18.0 38 A GLY N 249 210.1 104.2 18.9 37 A GLY CA 249 209.5 103.4 19.8 38 A GLY C 249 210.5 102.9 20.9 39 A GLY O 249 211.7 103.2 20.8 39 A TYR N 250 210.0 102.3 21.9 40 A TYR CA 250 210.8 101.8 23.0 41 A TYR CB 250 210.2 102.1 24.3 40 A TYR CG 250 210.1 103.6 24.6 40 A TYR CD1 250 209.1 104.4 24.0 39 A TYR CE1 250 209.0 105.7 24.3 40 A TYR CD2 250 210.9 104.2 25.6 40 A TYR CE2 250 210.8 105.5 25.9 40 A TYR CZ 250 209.9 106.3 25.2 40 A TYR OH 250 209.7 107.6 25.6 41 A TYR C 250 211.2 100.4 22.9 43 A TYR O 250 211.9  99.8 23.8 43 A SER N 251 210.7  99.7 21.9 44 A SER CA 251 211.0  98.3 21.6 45 A SER CB 251 210.2  97.8 20.4 45 A SER OG 251 208.8  98.0 20.7 46 A SER C 251 212.5  98.1 21.4 46 A SER O 251 213.1  97.2 22.0 46 A ASP N 252 213.0  99.0 20.5 47 A ASP CA 252 214.4  98.9 20.2 49 A ASP CB 252 214.8 100.1 19.3 51 A ASP CG 252 216.2 100.0 18.7 53 A ASP OD1 252 216.9  99.0 18.9 54 A ASP OD2 252 216.5 100.9 17.9 55 A ASP C 252 215.2  99.0 21.5 49 A ASP O 252 215.3 100.0 22.2 49 A ARG N 253 215.8  97.9 21.9 49 A ARG CA 253 216.6  97.7 23.1 48 A ARG CB 253 217.3  96.3 23.1 51 A ARG CG 253 216.4  95.1 23.2 54 A ARG CD 253 217.2  93.8 23.0 57 A ARG NE 253 216.5  92.6 23.4 59 A ARG CZ 253 216.5  91.5 22.8 60 A ARG NH1 253 217.3  91.3 21.7 60 A ARG NH2 253 215.8  90.5 23.2 60 A ARG C 253 217.7  98.8 23.3 46 A ARG O 253 218.0  99.1 24.5 45 A ALA N 254 218.2  99.3 22.2 44 A ALA CA 254 219.2 100.3 22.2 42 A ALA CB 254 219.8 100.5 20.9 43 A ALA C 254 218.6 101.6 22.7 42 A ALA O 254 219.1 102.3 23.5 41 A VAL N 255 217.4 101.9 22.1 41 A VAL CA 255 216.7 103.1 22.5 40 A VAL CB 255 215.5 103.4 21.6 40 A VAL CG1 255 214.8 104.7 22.0 41 A VAL CG2 255 215.9 103.4 20.2 40 A VAL C 255 216.3 103.0 23.9 40 A VAL O 255 216.5 103.8 24.8 40 A LEU N 256 215.6 101.9 24.2 39 A LEU CA 256 215.2 101.6 25.6 39 A LEU CB 256 214.6 100.2 25.7 38 A LEU CG 256 214.0  99.6 26.9 37 A LEU CD1 256 213.1 100.5 27.7 37 A LEU CD2 256 213.2  98.4 26.5 37 A LEU C 256 216.3 101.8 26.6 40 A LEU O 256 216.2 102.7 27.5 40 A GLU N 257 217.4 101.1 26.4 41 A GLU CA 257 218.6 101.2 27.3 42 A GLU CB 257 219.7 100.4 26.7 43 A GLU CG 257 221.1 100.6 27.2 46 A GLU CD 257 221.4 100.0 28.6 49 A GLU OE1 257 220.5 100.0 29.5 50 A GLU OE2 257 222.5  99.5 28.7 50 A GLU C 257 219.0 102.7 27.5 41 A GLU O 257 219.2 103.1 28.6 40 A ARG N 258 219.2 103.4 26.4 40 A ARG CA 258 219.6 104.8 26.3 40 A ARG CB 258 219.6 105.3 24.9 39 A ARG CG 258 220.0 106.8 24.8 39 A ARG CD 258 219.6 107.4 23.5 38 A ARG NE 258 218.1 107.6 23.4 39 A ARG CZ 258 217.4 107.6 22.3 39 A ARG NH1 258 218.0 107.5 21.1 39 A ARG NH2 258 216.1 107.7 22.4 39 A ARG C 258 218.8 105.7 27.2 40 A ARG O 258 219.3 106.6 27.9 41 A GLU N 259 217.5 105.5 27.1 40 A GLU CA 259 216.5 106.3 27.8 39 A GLU CB 259 215.1 106.0 27.3 39 A GLU CG 259 214.8 106.6 25.9 39 A GLU CD 259 215.0 108.1 26.0 39 A GLU OE1 259 214.4 108.8 26.9 40 A GLU OE2 259 215.7 108.7 25.1 39 A GLU C 259 216.5 105.9 29.3 40 A GLU O 259 216.6 106.7 30.1 40 A VAL N 260 216.6 104.6 29.5 41 A VAL CA 260 216.6 104.0 30.9 41 A VAL CB 260 216.5 102.5 30.9 41 A VAL CG1 260 216.8 102.0 32.3 41 A VAL CG2 260 215.1 102.1 30.6 41 A VAL C 260 217.8 104.5 31.6 42 A VAL O 260 217.7 104.9 32.8 42 A GLN N 261 219.0 104.6 30.9 42 A GLN CA 261 220.2 105.0 31.5 43 A GLN CB 261 221.3 104.8 30.5 46 A GLN CG 261 222.7 104.5 31.2 49 A GLN CD 261 222.8 103.1 31.8 50 A GLN OE1 261 222.7 102.1 31.0 50 A GLN NE2 261 223.0 102.9 33.1 51 A GLN C 261 220.1 106.5 31.8 42 A GLN O 261 220.2 106.9 33.0 42 A TYR N 262 219.9 107.3 30.8 40 A TYR CA 262 219.7 108.8 30.9 38 A TYR CB 262 219.1 109.3 29.6 38 A TYR CG 262 218.6 110.7 29.8 38 A TYR CD1 262 219.4 111.8 30.1 38 A TYR CE1 262 219.0 113.1 30.3 38 A TYR CD2 262 217.2 111.0 29.6 38 A TYR CE2 262 216.8 112.3 29.8 38 A TYR CZ 262 217.6 113.3 30.1 38 A TYR OH 262 217.2 114.6 30.3 38 A TYR C 262 218.8 109.2 32.0 38 A TYR O 262 219.1 110.1 32.8 37 A THR N 263 217.6 108.6 32.0 37 A THR CA 263 216.6 108.9 33.0 37 A THR CB 263 215.3 108.1 32.8 36 A THR OG1 263 214.9 108.2 31.4 35 A THR CG2 263 214.2 108.6 33.6 35 A THR C 263 217.1 108.6 34.4 38 A THR O 263 217.0 109.4 35.3 37 A LEU N 264 217.8 107.4 34.6 40 A LEU CA 264 218.3 107.0 35.9 42 A LEU CB 264 219.0 105.6 35.8 42 A LEU CG 264 218.1 104.4 36.0 41 A LEU CD1 264 218.8 103.2 35.7 41 A LEU CD2 264 217.4 104.4 37.4 41 A LEU C 264 219.4 108.1 36.2 44 A LEU O 264 219.5 108.5 37.4 44 A GLU N 265 220.1 108.5 35.2 46 A GLU CA 265 221.2 109.6 35.4 49 A GLU CB 265 221.9 109.9 34.1 52 A GLU CG 265 222.4 108.6 33.3 56 A GLU CD 265 223.3 107.7 34.1 59 A GLU OE1 265 222.8 106.5 34.4 60 A GLU OE2 265 224.4 108.1 34.5 61 A GLU C 265 220.5 110.8 36.0 49 A GLU O 265 221.1 111.5 36.9 50 A MET N 266 219.3 111.2 35.5 49 A MET CA 266 218.6 112.3 35.9 48 A MET CB 266 217.4 112.6 34.9 47 A MET CG 266 217.8 112.8 33.5 46 A MET SD 266 219.3 113.9 33.4 46 A MET CE 266 218.6 115.4 32.9 47 A MET C 266 218.1 112.1 37.3 48 A MET O 266 218.0 113.1 38.1 48 A ILE N 267 217.7 110.9 37.6 48 A ILE CA 267 217.2 110.5 38.9 49 A ILE CB 267 216.7 109.1 39.0 48 A ILE CG2 267 216.2 108.8 40.4 48 A ILE CG1 267 215.4 109.0 38.0 48 A ILE CD1 267 214.8 107.6 38.0 48 A ILE C 267 218.4 110.7 39.9 50 A ILE O 267 218.2 111.2 41.0 51 A LYS N 268 219.6 110.3 39.5 51 A LYS CA 268 220.7 110.5 40.4 52 A LYS CB 268 222.0 109.9 39.7 55 A LYS CG 268 221.9 108.4 39.6 58 A LYS CD 268 223.2 107.8 39.0 60 A LYS CE 268 222.9 106.3 38.7 62 A LYS NZ 268 223.9 105.7 37.7 63 A LYS C 268 220.9 112.0 40.7 51 A LYS O 268 220.9 112.3 41.9 52 A LEU N 269 220.8 112.8 39.7 51 A LEU CA 269 221.0 114.2 39.9 49 A LEU CB 269 221.2 115.0 38.6 50 A LEU CG 269 222.2 114.6 37.5 50 A LEU CD1 269 222.8 115.8 36.9 51 A LEU CD2 269 223.2 113.6 38.0 51 A LEU C 269 219.9 114.9 40.7 48 A LEU O 269 220.3 115.7 41.7 49 A VAL N 270 218.7 114.7 40.4 46 A VAL CA 270 217.6 115.3 41.2 44 A VAL CB 270 216.8 116.4 40.3 43 A VAL CG1 270 216.0 117.3 41.2 42 A VAL CG2 270 217.8 117.2 39.5 42 A VAL C 270 216.7 114.2 41.7 43 A VAL O 270 215.5 114.1 41.2 43 A PRO N 271 217.1 113.5 42.7 43 A PRO CD 271 218.3 113.7 43.4 43 A PRO CA 271 216.4 112.3 43.3 43 A PRO CB 271 217.2 112.0 44.5 43 A PRO CG 271 218.5 112.3 44.0 42 A PRO C 271 214.9 112.6 43.6 43 A PRO O 271 214.1 111.6 43.7 43 A HIS N 272 214.5 113.8 43.9 43 A HIS CA 272 213.2 114.2 44.3 43 A HIS CB 272 213.2 115.1 45.5 44 A HIS CG 272 213.7 114.4 46.8 46 A HIS CD2 272 214.9 114.4 47.3 46 A HIS ND1 272 212.8 113.7 47.6 47 A HIS CE1 272 213.5 113.2 48.6 47 A HIS NE2 272 214.8 113.6 48.5 47 A HIS C 272 212.3 114.7 43.2 41 A HIS O 272 211.3 115.3 43.4 41 A ASN N 273 212.8 114.6 41.9 39 A ASN CA 273 212.1 115.1 40.7 37 A ASN CB 273 213.1 115.5 39.6 36 A ASN CG 273 212.4 115.8 38.3 35 A ASN OD1 273 211.2 116.2 38.3 34 A ASN ND2 273 213.1 115.7 37.2 34 A ASN C 273 211.2 114.0 40.2 36 A ASN O 273 211.7 113.0 39.7 35 A GLU N 274 210.0 114.2 40.4 35 A GLU CA 274 209.0 113.2 40.0 34 A GLU CB 274 207.6 113.6 40.5 35 A GLU CG 274 206.6 112.6 40.3 37 A GLU CD 274 205.3 113.0 40.9 39 A GLU OE1 274 204.2 112.6 40.3 41 A GLU OE2 274 205.3 113.6 42.0 40 A GLU C 274 208.9 112.9 38.5 33 A GLU O 274 208.5 111.8 38.2 34 A SER N 275 209.2 113.9 37.7 33 A SER CA 275 209.0 113.7 36.2 33 A SER CB 275 209.3 114.9 35.5 33 A SER OG 275 208.5 116.0 35.9 33 A SER C 275 209.9 112.5 35.7 34 A SER O 275 209.5 111.6 35.0 34 A ALA N 276 211.2 112.6 36.1 34 A ALA CA 276 212.1 111.5 35.6 33 A ALA CB 276 213.5 111.8 36.2 33 A ALA C 276 211.6 110.2 36.2 33 A ALA O 276 211.7 109.2 35.5 33 A TRP N 277 211.1 110.2 37.4 33 A TRP CA 277 210.5 109.0 38.0 32 A TRP CB 277 210.2 109.3 39.4 33 A TRP CG 277 211.3 109.1 40.3 35 A TRP CD2 277 212.0 107.9 40.7 36 A TRP CE2 277 212.9 108.2 41.7 36 A TRP CE3 277 211.8 106.5 40.3 36 A TRP CD1 277 211.9 110.1 41.1 35 A TRP NE1 277 212.9 109.5 41.9 36 A TRP CZ2 277 213.8 107.2 42.2 36 A TRP CZ3 277 212.7 105.6 40.8 36 A TRP CH2 277 213.6 105.9 41.8 36 A TRP C 277 209.3 108.4 37.2 31 A TRP O 277 209.3 107.3 36.9 31 A ASN N 278 208.3 109.3 37.0 30 A ASN CA 278 207.1 108.9 36.3 29 A ASN CB 278 206.1 110.0 36.3 30 A ASN CG 278 205.6 110.4 37.6 30 A ASN OD1 278 206.0 109.8 38.6 30 A ASN ND2 278 204.8 111.5 37.7 31 A ASN C 278 207.5 108.5 34.9 29 A ASN O 278 206.7 107.8 34.2 29 A TYR N 279 208.6 109.0 34.4 28 A TYR CA 279 209.0 108.6 33.0 27 A TYR CB 279 210.0 109.7 32.5 26 A TYR CG 279 210.4 109.4 31.0 25 A TYR CD1 279 209.5 109.7 30.0 24 A TYR CE1 279 209.8 109.4 28.7 24 A TYR CD2 279 211.6 108.9 30.7 25 A TYR CE2 279 212.0 108.7 29.4 24 A TYR CZ 279 211.1 109.0 28.4 24 A TYR OH 279 211.6 108.8 27.1 24 A TYR C 279 209.6 107.3 33.0 27 A TYR O 279 209.4 106.5 32.1 28 A LEU N 280 210.4 107.0 34.1 28 A LEU CA 280 211.1 105.7 34.2 29 A LEU CB 280 211.9 105.6 35.5 28 A LEU CG 280 212.8 104.4 35.7 27 A LEU CD1 280 213.7 104.1 34.5 26 A LEU CD2 280 213.6 104.5 37.0 25 A LEU C 280 210.1 104.6 34.2 31 A LEU O 280 210.1 103.7 33.4 31 A LYS N 281 209.1 104.8 35.1 33 A LYS CA 281 208.0 103.8 35.2 35 A LYS CB 281 207.1 104.3 36.4 34 A LYS CG 281 206.0 103.2 36.7 35 A LYS CD 281 205.4 103.5 38.0 37 A LYS CE 281 204.6 104.8 38.0 38 A LYS NZ 281 204.5 105.5 39.3 39 A LYS C 281 207.2 103.8 34.0 36 A LYS O 281 206.9 102.7 33.5 37 A GLY N 282 206.9 104.9 33.3 37 A GLY CA 282 206.2 105.0 32.1 38 A GLY C 282 206.7 104.1 31.0 39 A GLY O 282 205.9 103.4 30.4 39 A ILE N 283 208.0 104.1 30.7 40 A ILE CA 283 208.6 103.4 29.6 41 A ILE CB 283 209.9 104.1 29.1 40 A ILE CG2 283 209.6 105.5 28.8 41 A ILE CG1 283 211.0 104.1 30.1 40 A ILE CD1 283 212.2 104.7 29.6 39 A ILE C 283 208.8 101.9 29.9 43 A ILE O 283 208.8 101.1 28.9 44 A LEU N 284 209.0 101.5 31.1 45 A LEU CA 284 209.3 100.1 31.5 47 A LEU CB 284 210.2  99.9 32.6 46 A LEU CG 284 211.6 100.6 32.5 45 A LEU CD1 284 212.3 100.4 33.9 46 A LEU CD2 284 212.5  99.9 31.4 45 A LEU C 284 208.0  99.4 31.8 49 A LEU O 284 207.7  98.2 31.4 49 A GLN N 285 207.1 100.1 32.6 52 A GLN CA 285 205.8  99.6 33.0 55 A GLN CB 285 204.9 100.7 33.7 56 A GLN CG 285 204.2 101.5 32.6 57 A GLN CD 285 203.2 102.6 33.2 59 A GLN OE1 285 202.5 103.2 32.5 59 A GLN NE2 285 203.2 102.7 34.6 59 A GLN C 285 205.0  99.0 31.9 56 A GLN O 285 204.0  98.4 32.2 57 A ASP N 286 205.4  99.2 30.7 58 A ASP CA 286 204.6  98.6 29.6 60 A ASP CB 286 204.4  99.6 28.5 63 A ASP CG 286 202.9  99.9 28.2 65 A ASP OD1 286 202.5  99.7 27.0 66 A ASP OD2 286 202.1 100.2 29.1 66 A ASP C 286 205.1  97.3 29.1 60 A ASP O 286 204.9  96.9 27.9 61 A ARG N 287 205.9  96.6 29.9 59 A ARG CA 287 206.4  95.2 29.6 59 A ARG CB 287 207.7  95.3 28.8 60 A ARG CG 287 208.2  93.9 28.2 61 A ARG CD 287 209.7  93.9 27.9 62 A ARG NE 287 210.3  92.7 28.3 63 A ARG CZ 287 211.3  92.0 27.5 63 A ARG NH1 287 211.7  92.5 26.4 62 A ARG NH2 287 211.7  90.8 28.0 63 A ARG C 287 206.6  94.4 30.9 58 A ARG O 287 206.8  93.2 30.9 58 A GLY N 288 206.5  95.1 32.0 56 A GLY CA 288 206.6  94.5 33.3 54 A GLY C 288 207.9  94.9 34.0 52 A GLY O 288 209.0  94.6 33.5 53 A LEU N 289 207.8  95.6 35.1 51 A LEU CA 289 209.1  96.0 35.8 50 A LEU CB 289 208.7  96.8 37.0 49 A LEU CG 289 208.7  98.4 36.9 48 A LEU CD1 289 208.5  98.8 35.4 48 A LEU CD2 289 207.6  98.9 37.7 48 A LEU C 289 209.9  94.8 36.2 50 A LEU O 289 211.1  94.9 36.4 50 A SER N 290 209.2  93.6 36.4 50 A SER CA 290 209.8  92.4 36.8 50 A SER CB 290 208.8  91.4 37.3 50 A SER OG 290 207.8  91.1 36.4 49 A SER C 290 210.7  91.7 35.7 50 A SER O 290 211.5  90.8 36.0 49 A ARG N 291 210.5  92.2 34.4 50 A ARG CA 291 211.3  91.6 33.3 50 A ARG CB 291 210.6  91.8 32.0 52 A ARG CG 291 209.8  90.5 31.7 55 A ARG CD 291 209.1  90.7 30.4 59 A ARG NE 291 208.8  89.4 29.7 63 A ARG CZ 291 208.7  89.2 28.4 65 A ARG NH1 291 208.5  88.0 27.9 66 A ARG NH2 291 208.9  90.3 27.6 66 A ARG C 291 212.7  92.3 33.2 49 A ARG O 291 213.4  92.2 32.2 49 A TYR N 292 213.0  93.1 34.3 47 A TYR CA 292 214.2  93.8 34.4 45 A TYR CB 292 213.9  95.3 34.2 42 A TYR CG 292 213.3  95.5 32.8 39 A TYR CD1 292 212.0  95.8 32.7 38 A TYR CE1 292 211.4  95.9 31.4 37 A TYR CD2 292 214.1  95.4 31.6 38 A TYR CE2 292 213.5  95.5 30.4 37 A TYR CZ 292 212.1  95.7 30.3 36 A TYR OH 292 211.6  95.8 29.0 34 A TYR C 292 214.8  93.6 35.8 46 A TYR O 292 214.7  94.4 36.7 46 A PRO N 293 215.4  92.4 36.0 46 A PRO CD 293 215.7  91.4 34.8 45 A PRO CA 293 216.0  91.9 37.2 46 A PRO CB 293 216.6  90.5 36.8 46 A PRO CG 293 216.9  90.7 35.3 45 A PRO C 293 217.1  92.7 37.8 47 A PRO O 293 217.3  92.7 39.0 48 A ASN N 294 217.9  93.5 37.0 48 A ASN CA 294 219.0  94.3 37.5 50 A ASN CB 294 219.9  94.8 36.4 49 A ASN CG 294 220.5  93.6 35.7 48 A ASN OD1 294 220.1  93.3 34.5 48 A ASN ND2 294 221.5  92.9 36.2 48 A ASN C 294 218.4  95.6 38.2 51 A ASN O 294 218.9  96.0 39.2 51 A LEU N 295 217.3  96.1 37.6 53 A LEU CA 295 216.6  97.3 38.0 55 A LEU CB 295 215.3  97.4 37.3 56 A LEU CG 295 214.5  98.7 37.2 57 A LEU CD1 295 215.3  99.7 36.5 57 A LEU CD2 295 213.2  98.4 36.5 57 A LEU C 295 216.5  97.4 39.5 55 A LEU O 295 216.9  98.4 40.1 54 A LEU N 296 215.8  96.4 40.1 56 A LEU CA 296 215.6  96.4 41.6 57 A LEU CB 296 215.0  95.1 42.1 56 A LEU CG 296 214.6  95.1 43.6 56 A LEU CD1 296 213.6  96.1 43.9 56 A LEU CD2 296 214.1  93.7 43.9 56 A LEU C 296 216.9  96.7 42.4 59 A LEU O 296 216.9  97.5 43.3 59 A ASN N 297 218.0  96.1 41.9 62 A ASN CA 297 219.3  96.2 42.5 65 A ASN CB 297 220.4  95.5 41.8 67 A ASN CG 297 220.1  94.0 41.5 69 A ASN OD1 297 218.9  93.6 41.5 70 A ASN ND2 297 221.1  93.2 41.3 69 A ASN C 297 219.6  97.7 42.6 65 A ASN O 297 219.4  98.4 43.6 65 A GLN N 298 220.0  98.3 41.4 66 A GLN CA 298 220.4  99.7 41.3 66 A GLN CB 298 220.3 100.1 39.8 66 A GLN CG 298 219.9  99.0 38.8 66 A GLN CD 298 221.0  98.2 38.3 66 A GLN OE1 298 221.5  97.3 39.1 66 A GLN NE2 298 221.4  98.3 37.1 65 A GLN C 298 219.6 100.6 42.1 67 A GLN O 298 220.1 101.3 43.0 68 A LEU N 299 218.2 100.5 42.0 68 A LEU CA 299 217.4 101.4 42.8 69 A LEU CB 299 215.9 101.1 42.5 68 A LEU CG 299 215.3 101.4 41.1 68 A LEU CD1 299 213.8 101.2 41.2 68 A LEU CD2 299 215.7 102.8 40.7 67 A LEU C 299 217.6 101.2 44.3 69 A LEU O 299 217.8 102.2 45.0 68 A LEU N 300 217.7  99.9 44.7 71 A LEU CA 300 218.0  99.6 46.1 72 A LEU CB 300 218.0  98.1 46.2 72 A LEU CG 300 216.8  97.2 46.7 73 A LEU CD1 300 215.6  97.9 46.2 74 A LEU CD2 300 217.0  95.8 46.2 73 A LEU C 300 219.3 100.2 46.5 73 A LEU O 300 219.4 100.6 47.7 73 A ASP N 301 220.3 100.2 45.6 75 A ASP CA 301 221.6 100.7 45.9 76 A ASP CB 301 222.5 100.5 44.7 76 A ASP CG 301 222.8  99.0 44.4 77 A ASP OD1 301 222.2  98.1 45.1 77 A ASP OD2 301 223.5  98.6 43.4 77 A ASP C 301 221.5 102.2 46.2 77 A ASP O 301 222.2 102.6 47.2 77 A LEU N 302 220.7 102.9 45.5 77 A LEU CA 302 220.6 104.4 45.8 78 A LEU CB 302 219.9 105.1 44.6 79 A LEU CG 302 220.7 105.2 43.3 79 A LEU CD1 302 220.0 106.1 42.2 79 A LEU CD2 302 222.1 105.7 43.5 79 A LEU C 302 219.8 104.7 47.0 78 A LEU O 302 219.7 105.8 47.5 78 A GLN N 303 219.2 103.6 47.6 79 A GLN CA 303 218.4 103.8 48.9 80 A GLN CB 303 218.2 102.4 49.5 79 A GLN CG 303 216.9 101.7 49.1 80 A GLN CD 303 215.7 102.3 49.8 80 A GLN OE1 303 215.6 103.5 49.9 79 A GLN NE2 303 214.8 101.4 50.3 80 A GLN C 303 219.0 104.7 49.8 81 A GLN O 303 218.4 105.7 50.3 81 A PRO N 304 220.3 104.5 50.2 82 A PRO CD 304 221.2 103.4 49.9 81 A PRO CA 304 220.9 105.4 51.2 82 A PRO CB 304 222.1 104.7 51.6 82 A PRO CG 304 222.5 103.9 50.4 82 A PRO C 304 221.3 106.8 50.6 82 A PRO O 304 220.9 107.8 51.1 82 A SER N 305 222.0 106.8 49.4 82 A SER CA 305 222.4 108.0 48.8 82 A SER CB 305 223.8 107.8 48.0 82 A SER OG 305 223.7 106.7 47.1 83 A SER C 305 221.5 108.9 48.0 82 A SER O 305 221.4 110.1 48.1 82 A HIS N 306 220.7 108.2 47.1 81 A HIS CA 306 219.7 109.0 46.3 80 A HIS CB 306 220.0 108.8 44.8 81 A HIS CG 306 221.4 109.2 44.4 82 A HIS CD2 306 222.1 108.9 43.3 82 A HIS ND1 306 222.1 110.1 45.1 82 A HIS CE1 306 223.3 110.3 44.6 82 A HIS NE2 306 223.3 109.6 43.4 82 A HIS C 306 218.3 108.7 46.6 79 A HIS O 306 217.4 108.5 45.8 80 A SER N 307 218.0 108.7 47.9 78 A SER CA 307 216.7 108.4 48.5 76 A SER CB 307 216.9 108.3 50.0 76 A SER OG 307 215.9 107.4 50.6 76 A SER C 307 215.7 109.5 48.2 75 A SER O 307 216.0 110.6 48.0 76 A SER N 308 214.4 109.0 48.1 73 A SER CA 308 213.3 109.9 47.8 70 A SER CB 308 213.4 110.5 46.4 70 A SER OG 308 213.1 109.6 45.4 69 A SER C 308 212.1 109.0 47.9 68 A SER O 308 212.1 107.9 47.4 69 A PRO N 309 210.9 109.5 48.4 66 A PRO CD 309 210.5 110.8 48.8 66 A PRO CA 309 209.8 108.6 48.5 64 A PRO CB 309 208.7 109.5 49.1 65 A PRO CG 309 209.0 110.8 48.6 65 A PRO C 309 209.3 108.0 47.1 63 A PRO O 309 208.5 107.1 47.0 62 A TYR N 310 210.0 108.5 46.0 60 A TYR CA 310 209.7 108.0 44.7 57 A TYR CB 310 210.2 109.1 43.7 57 A TYR CG 310 209.7 110.4 44.0 57 A TYR CD1 310 210.5 111.4 44.6 57 A TYR CE1 310 209.9 112.6 45.0 58 A TYR CD2 310 208.3 110.7 43.8 56 A TYR CE2 310 207.8 111.9 44.2 57 A TYR CZ 310 208.6 112.9 44.8 58 A TYR OH 310 208.0 114.0 45.3 59 A TYR C 310 210.4 106.7 44.5 55 A TYR O 310 209.9 105.8 43.7 55 A LEU N 311 211.6 106.5 45.1 52 A LEU CA 311 212.3 105.3 45.0 49 A LEU CB 311 213.7 105.5 45.7 49 A LEU CG 311 214.7 104.3 45.8 49 A LEU CD1 311 215.2 104.0 44.4 49 A LEU CD2 311 215.9 104.7 46.6 49 A LEU C 311 211.6 104.3 45.8 47 A LEU O 311 211.3 103.2 45.3 46 A ILE N 312 211.1 104.6 47.0 46 A ILE CA 312 210.4 103.7 47.9 45 A ILE CB 312 209.9 104.4 49.2 45 A ILE CG2 312 209.1 103.4 50.1 45 A ILE CG1 312 211.0 104.9 50.1 46 A ILE CD1 312 211.9 103.9 50.7 46 A ILE C 312 209.2 103.2 47.1 44 A ILE O 312 209.0 102.0 47.1 45 A ALA N 313 208.4 104.1 46.5 43 A ALA CA 313 207.2 103.7 45.8 41 A ALA CB 313 206.3 104.9 45.5 41 A ALA C 313 207.5 102.9 44.5 39 A ALA O 313 206.7 102.1 44.0 39 A PHE N 314 208.7 103.1 43.9 38 A PHE CA 314 209.1 102.4 42.7 38 A PHE CB 314 210.4 103.0 42.0 37 A PHE CG 314 210.5 102.7 40.5 37 A PHE CD1 314 210.4 103.7 39.6 37 A PHE CD2 314 210.6 101.4 40.1 37 A PHE CE1 314 210.5 103.4 38.2 37 A PHE CE2 314 210.6 101.1 38.7 37 A PHE CZ 314 210.6 102.1 37.8 37 A PHE C 314 209.2 100.9 43.1 38 A PHE O 314 208.7 100.0 42.4 39 A LEU N 315 209.9 100.7 44.2 37 A LEU CA 315 210.2  99.3 44.6 36 A LEU CB 315 210.9  99.3 46.0 35 A LEU CG 315 212.2 100.1 45.9 35 A LEU CD1 315 212.9 100.2 47.3 34 A LEU CD2 315 213.2  99.6 44.9 34 A LEU C 315 208.9  98.6 44.8 36 A LEU O 315 208.8  97.5 44.3 37 A VAL N 316 207.9  99.2 45.4 37 A VAL CA 316 206.6  98.6 45.5 38 A VAL CB 316 205.5  99.5 46.2 37 A VAL CG1 316 204.2  98.7 46.3 37 A VAL CG2 316 206.0  99.8 47.6 37 A VAL C 316 206.0  98.3 44.1 39 A VAL O 316 205.4  97.2 43.9 39 A ASP N 317 206.2  99.2 43.2 40 A ASP CA 317 205.8  99.0 41.8 41 A ASP CB 317 206.0 100.2 40.9 42 A ASP CG 317 205.2 101.4 41.3 43 A ASP OD1 317 204.0 101.2 41.7 44 A ASP OD2 317 205.7 102.5 41.3 44 A ASP C 317 206.5  97.7 41.2 41 A ASP O 317 205.9  97.1 40.4 40 A ILE N 318 207.7  97.5 41.5 41 A ILE CA 318 208.4  96.3 41.0 42 A ILE CB 318 210.0  96.4 41.3 42 A ILE CG2 318 210.6  95.1 40.9 42 A ILE CG1 318 210.6  97.6 40.7 41 A ILE CD1 318 212.1  97.6 40.8 40 A ILE C 318 207.9  95.1 41.7 43 A ILE O 318 207.5  94.2 41.0 44 A TYR N 319 207.8  95.1 43.0 45 A TYR CA 319 207.3  94.0 43.7 48 A TYR CB 319 207.3  94.3 45.2 48 A TYR CG 319 208.6  94.5 45.8 48 A TYR CD1 319 208.8  95.1 47.1 48 A TYR CE1 319 210.1  95.3 47.6 48 A TYR CD2 319 209.8  94.0 45.2 48 A TYR CE2 319 211.0  94.2 45.7 48 A TYR CZ 319 211.2  94.8 46.9 48 A TYR OH 319 212.4  94.9 47.5 49 A TYR C 319 205.9  93.6 43.3 50 A TYR O 319 205.7  92.4 43.0 51 A GLU N 320 205.0  94.6 43.1 52 A GLU CA 320 203.7  94.3 42.6 54 A GLU CB 320 202.9  95.6 42.4 56 A GLU CG 320 202.6  96.5 43.6 58 A GLU CD 320 202.4  98.0 43.3 60 A GLU OE1 320 201.7  98.7 44.2 61 A GLU OE2 320 202.8  98.5 42.3 61 A GLU C 320 203.7  93.5 41.3 53 A GLU O 320 203.1  92.5 41.2 53 A ASP N 321 204.6  93.9 40.4 54 A ASP CA 321 204.7  93.2 39.2 55 A ASP CB 321 205.4  94.0 38.1 53 A ASP CG 321 205.3  93.4 36.7 53 A ASP OD1 321 204.1  93.2 36.3 53 A ASP OD2 321 206.3  93.1 36.1 52 A ASP C 321 205.3  91.8 39.3 56 A ASP O 321 205.0  91.0 38.5 57 A MET N 322 206.2  91.7 40.2 58 A MET CA 322 206.9  90.4 40.4 60 A MET CB 322 208.0  90.5 41.3 59 A MET CG 322 209.2  91.3 40.8 58 A MET SD 322 210.8  91.0 41.5 57 A MET CE 322 210.7  91.6 43.1 56 A MET C 322 205.8  89.3 40.8 62 A MET O 322 205.8  88.3 40.3 62 A LEU N 323 205.0  89.7 41.8 65 A LEU CA 323 204.0  88.8 42.3 68 A LEU CB 323 203.2  89.4 43.4 68 A LEU CG 323 203.6  89.3 44.9 68 A LEU CD1 323 205.1  89.4 45.1 68 A LEU CD2 323 202.9  90.3 45.7 68 A LEU C 323 203.1  88.4 41.2 70 A LEU O 323 202.9  87.2 40.8 70 A GLU N 324 202.6  89.4 40.5 74 A GLU CA 324 201.7  89.3 39.3 77 A GLU CB 324 201.5  90.6 38.6 78 A GLU CG 324 200.6  91.6 39.5 80 A GLU CD 324 200.7  93.1 39.0 81 A GLU OE1 324 201.1  93.4 37.8 82 A GLU OE2 324 200.4  94.0 39.8 82 A GLU C 324 202.3  88.3 38.3 78 A GLU O 324 201.6  87.5 37.7 78 A ASN N 325 203.6  88.3 38.2 79 A ASN CA 325 204.3  87.4 37.3 80 A ASN CB 325 205.3  88.2 36.4 80 A ASN CG 325 204.6  89.3 35.5 81 A ASN OD1 325 205.0  90.4 35.4 81 A ASN ND2 325 203.4  88.9 35.0 81 A ASN C 325 205.1  86.3 37.9 81 A ASN O 325 206.2  86.0 37.6 81 A GLN N 326 204.4  85.6 38.9 83 A GLN CA 326 204.9  84.5 39.6 85 A GLN CB 326 204.6  83.2 38.8 85 A GLN CG 326 203.2  83.1 38.2 86 A GLN CD 326 203.0  83.3 36.7 86 A GLN OE1 326 203.7  82.6 35.9 86 A GLN NE2 326 202.2  84.2 36.3 86 A GLN C 326 206.4  84.5 40.1 85 A GLN O 326 207.1  83.6 39.7 85 A CYS N 327 206.8  85.5 40.8 86 A CYS CA 327 208.1  85.6 41.3 87 A CYS CB 327 208.4  87.0 41.8 87 A CYS SG 327 207.9  87.3 43.5 86 A CYS C 327 208.4  84.7 42.4 89 A CYS O 327 207.5  84.3 43.2 89 A ASP N 328 209.7  84.2 42.5 90 A ASP CA 328 210.0  83.2 43.5 91 A ASP CB 328 211.2  82.3 43.1 92 A ASP CG 328 210.9  80.9 43.5 93 A ASP OD1 328 210.6  80.0 42.6 93 A ASP OD2 328 210.9  80.5 44.7 93 A ASP C 328 210.4  84.1 44.7 91 A ASP O 328 211.0  85.1 44.6 91 A ASN N 329 209.9  83.7 45.9 91 A ASN CA 329 210.0  84.3 47.2 90 A ASN CB 329 211.2  85.3 47.2 90 A ASN CG 329 212.5  84.6 47.3 90 A ASN OD1 329 212.9  83.8 46.4 90 A ASN ND2 329 213.3  84.8 48.3 91 A ASN C 329 208.8  85.1 47.5 90 A ASN O 329 208.8  86.0 48.3 90 A LYS N 330 207.7  84.7 46.9 90 A LYS CA 330 206.4  85.3 47.0 90 A LYS CB 330 205.2  84.4 46.6 90 A LYS CG 330 204.3  85.0 45.5 91 A LYS CD 330 203.3  84.1 45.0 91 A LYS CE 330 202.4  84.7 43.9 91 A LYS NZ 330 203.2  85.1 42.7 90 A LYS C 330 206.1  85.8 48.5 90 A LYS O 330 205.9  87.0 48.7 89 A GLU N 331 206.3  84.9 49.4 90 A GLU CA 331 206.1  85.1 50.8 90 A GLU CB 331 206.5  83.9 51.7 92 A GLU CG 331 205.9  82.6 51.3 93 A GLU CD 331 204.6  82.3 52.0 94 A GLU OE1 331 203.8  81.4 51.6 94 A GLU OE2 331 204.3  83.0 53.0 95 A GLU C 331 207.0  86.3 51.3 89 A GLU O 331 206.6  87.2 51.9 88 A ASP N 332 208.3  86.2 50.9 87 A ASP CA 332 209.3  87.2 51.2 86 A ASP CB 332 210.7  86.6 50.8 87 A ASP CG 332 211.8  87.6 50.8 88 A ASP OD1 332 212.7  87.5 49.9 88 A ASP OD2 332 211.9  88.4 51.7 89 A ASP C 332 209.1  88.5 50.5 84 A ASP O 332 208.9  89.5 51.2 84 A ILE N 333 209.1  88.6 49.2 82 A ILE CA 333 208.9  89.8 48.4 79 A ILE CB 333 208.9  89.5 46.9 79 A ILE CG2 333 208.2  90.5 46.1 78 A ILE CG1 333 210.4  89.4 46.4 78 A ILE CD1 333 210.6  88.7 45.1 78 A ILE C 333 207.6  90.5 48.9 78 A ILE O 333 207.7  91.7 49.1 78 A LEU N 334 206.6  89.8 49.1 76 A LEU CA 334 205.3  90.4 49.5 75 A LEU CB 334 204.2  89.3 49.7 75 A LEU CG 334 202.9  89.7 50.4 74 A LEU CD1 334 202.2  90.8 49.6 74 A LEU CD2 334 202.1  88.5 50.4 74 A LEU C 334 205.5  91.2 50.8 75 A LEU O 334 205.0  92.3 50.8 76 A ASN N 335 206.1  90.6 51.8 75 A ASN CA 335 206.3  91.3 53.1 75 A ASN CB 335 207.1  90.5 54.1 76 A ASN CG 335 206.3  89.3 54.6 77 A ASN OD1 335 205.1  89.4 55.0 77 A ASN ND2 335 206.9  88.1 54.6 77 A ASN C 335 206.9  92.7 52.9 74 A ASN O 335 206.5  93.7 53.5 74 A LYS N 336 207.9  92.7 52.0 72 A LYS CA 336 208.6  94.0 51.8 71 A LYS CB 336 209.7  93.8 50.7 72 A LYS CG 336 211.1  93.9 51.3 72 A LYS CD 336 212.1  93.1 50.4 73 A LYS CE 336 211.7  91.6 50.4 73 A LYS NZ 336 212.7  90.8 49.6 74 A LYS C 336 207.6  95.0 51.2 70 A LYS O 336 207.4  96.0 51.9 69 A ALA N 337 207.0  94.6 50.1 68 A ALA CA 337 206.0  95.4 49.5 66 A ALA CB 337 205.2  94.6 48.4 66 A ALA C 337 205.0  96.0 50.5 65 A ALA O 337 204.7  97.2 50.5 65 A LEU N 338 204.5  95.2 51.4 64 A LEU CA 338 203.6  95.6 52.4 63 A LEU CB 338 202.9  94.4 53.1 63 A LEU CG 338 202.1  93.5 52.2 63 A LEU CD1 338 201.7  92.3 52.9 62 A LEU CD2 338 200.8  94.3 51.7 62 A LEU C 338 204.2  96.5 53.5 63 A LEU O 338 203.6  97.5 54.0 63 A GLU N 339 205.5  96.3 53.8 63 A GLU CA 339 206.2  97.1 54.8 63 A GLU CB 339 207.6  96.5 55.1 65 A GLU CG 339 208.3  97.2 56.2 68 A GLU CD 339 209.8  97.1 56.2 69 A GLU OE1 339 210.3  95.9 56.0 70 A GLU OE2 339 210.5  98.1 56.2 70 A GLU C 339 206.4  98.5 54.2 61 A GLU O 339 206.1  99.5 54.9 60 A LEU N 340 206.9  98.6 53.0 59 A LEU CA 340 207.1  99.8 52.3 57 A LEU CB 340 207.7  99.6 50.9 56 A LEU CG 340 209.0  98.7 50.8 56 A LEU CD1 340 209.5  98.7 49.3 56 A LEU CD2 340 210.1  99.3 51.7 56 A LEU C 340 205.8 100.5 52.2 57 A LEU O 340 205.7 101.7 52.5 57 A CYS N 341 204.7  99.8 51.9 56 A CYS CA 341 203.4 100.4 51.8 55 A CYS CB 341 202.3  99.4 51.4 55 A CYS SG 341 202.3  98.9 49.7 54 A CYS C 341 203.0 101.1 53.1 55 A CYS O 341 202.3 102.1 53.1 55 A GLU N 342 203.4 100.5 54.2 55 A GLU CA 342 203.1 101.0 55.5 55 A GLU CB 342 203.2  99.9 56.6 56 A GLU CG 342 202.3 100.3 57.8 57 A GLU CD 342 200.9 100.7 57.4 58 A GLU OE1 342 200.2 101.2 58.3 59 A GLU OE2 342 200.4 100.5 56.3 58 A GLU C 342 204.0 102.2 55.9 55 A GLU O 342 203.6 103.2 56.4 55 A ILE N 343 205.3 102.0 55.5 55 A ILE CA 343 206.3 103.1 55.8 54 A ILE CB 343 207.7 102.7 55.2 54 A ILE CG2 343 208.6 103.9 55.3 54 A ILE CG1 343 208.3 101.6 56.1 55 A ILE CD1 343 209.8 101.3 55.7 55 A ILE C 343 205.8 104.3 55.1 53 A ILE O 343 205.8 105.4 55.7 54 A LEU N 344 205.4 104.1 53.9 52 A LEU CA 344 204.9 105.2 53.0 52 A LEU CB 344 204.5 104.6 51.6 50 A LEU CG 344 205.7 104.3 50.7 49 A LEU CD1 344 205.2 103.9 49.4 48 A LEU CD2 344 206.5 105.6 50.5 49 A LEU C 344 203.6 105.8 53.7 53 A LEU O 344 203.6 107.0 53.9 53 A ALA N 345 202.6 105.0 54.0 54 A ALA CA 345 201.4 105.4 54.6 55 A ALA CB 345 200.4 104.3 54.6 55 A ALA C 345 201.5 106.0 56.0 56 A ALA O 345 200.8 107.0 56.3 56 A LYS N 346 202.4 105.5 56.8 58 A LYS CA 346 202.6 105.9 58.2 59 A LYS CB 346 203.1 104.8 59.1 61 A LYS CG 346 202.0 104.1 59.9 64 A LYS CD 346 202.6 103.0 60.9 65 A LYS CE 346 201.6 102.1 61.5 66 A LYS NZ 346 202.1 101.0 62.4 66 A LYS C 346 203.6 107.0 58.3 60 A LYS O 346 203.5 107.9 59.1 60 A GLU N 347 204.6 107.0 57.5 59 A GLU CA 347 205.7 108.0 57.6 59 A GLU CB 347 206.9 107.3 58.2 60 A GLU CG 347 208.2 108.2 58.2 62 A GLU CD 347 209.5 107.4 58.3 63 A GLU OE1 347 210.5 108.1 58.4 64 A GLU OE2 347 209.4 106.2 58.3 64 A GLU C 347 206.2 108.8 56.3 57 A GLU O 347 206.1 110.0 56.3 57 A LYS N 348 206.7 108.1 55.3 56 A LYS CA 348 207.3 108.7 54.1 54 A LYS CB 348 208.1 107.7 53.4 55 A LYS CG 348 209.2 107.0 54.2 56 A LYS CD 348 210.2 107.9 54.8 56 A LYS CE 348 211.3 107.2 55.6 57 A LYS NZ 348 212.0 106.1 54.8 57 A LYS C 348 206.4 109.4 53.2 52 A LYS O 348 206.8 110.4 52.5 52 A ASP N 349 205.1 109.0 53.0 50 A ASP CA 349 204.2 109.6 52.1 48 A ASP CB 349 204.3 108.9 50.8 49 A ASP CG 349 203.8 109.7 49.6 49 A ASP OD1 349 203.6 110.9 49.7 50 A ASP OD2 349 203.5 109.0 48.5 50 A ASP C 349 202.8 109.6 52.6 47 A ASP O 349 201.9 109.2 52.0 46 A THR N 350 202.6 110.3 53.8 46 A THR CA 350 201.3 110.3 54.4 46 A THR CB 350 201.5 110.8 55.9 46 A THR OG1 350 201.7 112.2 55.9 47 A THR CG2 350 202.7 110.2 56.6 46 A THR C 350 200.1 110.9 53.8 45 A THR O 350 199.0 110.5 54.0 46 A ILE N 351 200.3 112.0 53.0 45 A ILE CA 351 199.2 112.7 52.3 43 A ILE CB 351 199.7 113.8 51.4 42 A ILE CG2 351 200.4 113.2 50.1 41 A ILE CG1 351 198.6 114.8 51.1 41 A ILE CD1 351 198.4 115.7 52.2 40 A ILE C 351 198.3 111.6 51.5 42 A ILE O 351 197.1 111.8 51.4 41 A ARG N 352 198.9 110.5 51.2 42 A ARG CA 352 198.2 109.5 50.5 43 A ARG CB 352 198.7 109.3 49.0 43 A ARG CG 352 200.1 109.4 48.8 44 A ARG CD 352 200.4 110.0 47.4 44 A ARG NE 352 201.6 110.8 47.4 44 A ARG CZ 352 201.7 112.2 47.3 44 A ARG NH1 352 200.6 112.9 47.1 44 A ARG NH2 352 202.9 112.8 47.4 45 A ARG C 352 198.2 108.1 51.2 44 A ARG O 352 198.4 107.1 50.6 44 A LYS N 353 198.0 108.2 52.5 44 A LYS CA 353 198.0 107.0 53.4 44 A LYS CB 353 197.7 107.4 54.8 44 A LYS CG 353 196.3 108.0 55.0 44 A LYS CD 353 196.2 108.9 56.3 43 A LYS CE 353 194.9 109.7 56.3 42 A LYS NZ 353 194.9 110.7 57.4 42 A LYS C 353 196.9 106.1 52.8 45 A LYS O 353 197.0 104.9 52.7 44 A GLU N 354 195.8 106.8 52.5 45 A GLU CA 354 194.6 106.1 51.9 46 A GLU CB 354 193.6 107.1 51.5 47 A GLU CG 354 192.8 107.7 52.7 49 A GLU CD 354 192.0 106.8 53.4 50 A GLU OE1 354 192.3 106.4 54.6 51 A GLU OE2 354 190.9 106.3 52.9 50 A GLU C 354 195.0 105.2 50.7 46 A GLU O 354 194.5 104.0 50.6 46 A TYR N 355 195.7 105.8 49.7 44 A TYR CA 355 196.1 105.0 48.6 43 A TYR CB 355 196.7 105.9 47.5 41 A TYR CG 355 197.4 105.2 46.4 38 A TYR CD1 355 196.7 104.6 45.3 37 A TYR CE1 355 197.3 103.9 44.3 36 A TYR CD2 355 198.8 105.0 46.4 36 A TYR CE2 355 199.4 104.4 45.4 36 A TYR CZ 355 198.7 103.8 44.4 36 A TYR OH 355 199.4 103.2 43.4 36 A TYR C 355 197.1 103.9 49.0 44 A TYR O 355 196.8 102.7 48.7 45 A TRP N 356 198.2 104.3 49.6 46 A TRP CA 356 199.2 103.3 50.0 48 A TRP CB 356 200.4 104.1 50.6 47 A TRP CG 356 201.2 104.6 49.6 47 A TRP CD2 356 201.8 103.9 48.5 47 A TRP CE2 356 202.4 104.9 47.7 47 A TRP CE3 356 201.8 102.6 48.1 47 A TRP CD1 356 201.5 106.0 49.4 47 A TRP NE1 356 202.3 106.1 48.3 47 A TRP CZ2 356 203.1 104.5 46.5 47 A TRP CZ3 356 202.4 102.2 46.9 47 A TRP CH2 356 203.1 103.2 46.2 48 A TRP C 356 198.7 102.2 50.9 49 A TRP O 356 199.3 101.1 50.9 49 A ARG N 357 197.7 102.4 51.7 50 A ARG CA 357 197.1 101.3 52.5 51 A ARG CB 357 196.4 101.9 53.7 52 A ARG CG 357 197.3 102.0 54.9 55 A ARG CD 357 197.2 103.3 55.6 56 A ARG NE 357 195.8 103.6 56.0 58 A ARG CZ 357 195.4 104.4 57.0 59 A ARG NH1 357 194.1 104.5 57.3 59 A ARG NH2 357 196.3 105.1 57.7 58 A ARG C 357 196.3 100.4 51.7 50 A ARG O 357 196.3  99.2 51.9 51 A TYR N 358 195.6 101.0 50.7 50 A TYR CA 358 194.8 100.2 49.8 49 A TYR CB 358 194.1 101.1 48.8 48 A TYR CG 358 193.6 100.5 47.5 47 A TYR CD1 358 192.4  99.8 47.5 47 A TYR CE1 358 191.9  99.2 46.3 46 A TYR CD2 358 194.3 100.6 46.3 47 A TYR CE2 358 193.8 100.0 45.2 46 A TYR CZ 358 192.6  99.3 45.2 46 A TYR OH 358 192.2  98.7 44.0 46 A TYR C 358 195.7  99.2 49.0 49 A TYR O 358 195.2  98.2 48.6 48 A ILE N 359 196.9  99.7 48.7 51 A ILE CA 359 197.9  98.9 48.0 52 A ILE CB 359 199.2  99.7 47.7 50 A ILE CG2 359 200.3  98.8 47.3 50 A ILE CG1 359 198.8 100.6 46.5 50 A ILE CD1 359 198.3  99.9 45.3 49 A ILE C 359 198.3  97.7 49.0 53 A ILE O 359 198.5  96.6 48.5 52 A GLY N 360 198.4  98.0 50.2 54 A GLY CA 360 198.7  97.0 51.2 56 A GLY C 360 197.6  96.0 51.2 57 A GLY O 360 197.8  94.8 51.0 57 A ARG N 361 196.4  96.5 51.2 58 A ARG CA 361 195.2  95.7 51.2 59 A ARG CB 361 193.9  96.5 51.4 60 A ARG CG 361 193.2  96.4 52.7 61 A ARG CD 361 192.9  97.8 53.3 62 A ARG NE 361 192.0  98.5 52.5 63 A ARG CZ 361 192.0  99.9 52.3 64 A ARG NH1 361 191.2 100.5 51.5 64 A ARG NH2 361 193.0 100.6 53.0 64 A ARG C 361 195.0  94.8 50.0 60 A ARG O 361 194.8  93.6 50.1 60 A SER N 362 195.2  95.4 48.8 60 A SER CA 362 195.2  94.6 47.5 60 A SER CB 362 195.2  95.5 46.3 60 A SER OG 362 193.9  96.1 46.1 61 A SER C 362 196.3  93.6 47.5 60 A SER O 362 196.0  92.4 47.2 60 A LEU N 363 197.5  94.0 47.8 60 A LEU CA 363 198.6  93.1 47.8 61 A LEU CB 363 199.9  93.8 48.2 60 A LEU CG 363 200.8  94.3 47.1 59 A LEU CD1 363 200.1  94.9 46.0 59 A LEU CD2 363 201.8  95.3 47.7 59 A LEU C 363 198.3  92.0 48.7 61 A LEU O 363 198.8  90.8 48.5 61 A GLN N 364 197.5  92.3 49.7 63 A GLN CA 364 197.1  91.3 50.7 64 A GLN CB 364 196.4  92.0 51.9 65 A GLN CG 364 196.5  91.3 53.2 66 A GLN CD 364 198.0  91.3 53.7 66 A GLN OE1 364 198.3  92.1 54.6 67 A GLN NE2 364 198.9  90.6 53.0 66 A GLN C 364 196.3  90.2 50.2 65 A GLN O 364 196.1  89.2 50.8 66 A SER N 365 195.6  90.4 49.1 65 A SER CA 365 194.8  89.4 48.5 66 A SER CB 365 193.3  89.8 48.4 66 A SER OG 365 193.1  91.0 47.7 67 A SER C 365 195.2  88.9 47.2 68 A SER O 365 194.4  88.6 46.3 68 A LYS N 366 196.6  88.8 47.0 70 A LYS CA 366 197.2  88.3 45.7 72 A LYS CB 366 196.6  89.0 44.5 73 A LYS CG 366 196.7  90.5 44.4 74 A LYS CD 366 195.4  91.2 44.8 75 A LYS CE 366 194.2  90.8 44.1 76 A LYS NZ 366 192.9  91.5 44.5 77 A LYS C 366 198.8  88.4 45.7 72 A LYS OT1 366 199.3  87.9 46.7 72 A LYS OT2 366 199.4  88.8 44.7 71 A LEU CB 523 194.7 121.9 61.8 46 B LEU CG 523 193.4 122.7 62.0 46 B LEU CD1 523 193.7 124.2 61.8 47 B LEU CD2 523 192.3 122.1 61.1 46 B LEU C 523 195.9 119.7 61.6 47 B LEU O 523 197.0 119.9 62.1 46 B LEU N 523 194.6 120.2 63.5 48 B LEU CA 523 194.7 120.4 62.1 47 B TYR N 524 195.7 118.9 60.6 47 B TYR CA 524 196.8 118.1 60.0 47 B TYR CB 524 196.2 117.2 58.9 46 B TYR CG 524 197.3 116.4 58.1 47 B TYR CD1 524 198.0 115.3 58.6 46 B TYR CE1 524 198.9 114.6 57.8 46 B TYR CD2 524 197.5 116.8 56.8 46 B TYR CE2 524 198.4 116.1 56.0 46 B TYR CZ 524 199.1 115.0 56.5 46 B TYR OH 524 199.9 114.3 55.6 45 B TYR C 524 198.0 118.9 59.5 47 B TYR O 524 199.1 118.7 59.9 48 B SER N 525 197.7 119.9 58.6 48 B SER CA 525 198.7 120.7 58.0 50 B SER CB 525 198.1 121.6 57.0 49 B SER OG 525 196.8 122.0 57.4 50 B SER C 525 199.5 121.5 59.1 51 B SER O 525 200.7 121.8 58.9 51 B LEU N 526 198.9 121.8 60.2 52 B LEU CA 526 199.5 122.6 61.3 53 B LEU CB 526 198.5 123.3 62.1 54 B LEU CG 526 198.2 124.8 61.8 54 B LEU CD1 526 199.5 125.5 61.4 55 B LEU CD2 526 197.2 124.9 60.6 54 B LEU C 526 200.3 121.6 62.2 54 B LEU O 526 201.0 122.1 63.1 54 B ARG N 527 200.3 120.3 61.9 55 B ARG CA 527 201.0 119.4 62.7 57 B ARG CB 527 200.7 118.0 62.3 58 B ARG CG 527 201.0 116.9 63.3 59 B ARG CD 527 200.2 115.6 63.0 60 B ARG NE 527 198.8 115.8 63.1 61 B ARG CZ 527 197.9 115.1 62.5 61 B ARG NH1 527 198.3 114.1 61.7 61 B ARG NH2 527 196.6 115.3 62.7 61 B ARG C 527 202.5 119.6 62.5 58 B ARG O 527 203.0 119.9 61.4 59 B PRO N 528 203.3 119.5 63.6 59 B PRO CD 528 202.8 119.4 65.0 60 B PRO CA 528 204.8 119.7 63.6 59 B PRO CB 528 205.2 119.3 65.0 59 B PRO CG 528 204.0 119.8 65.8 60 B PRO C 528 205.6 119.0 62.6 60 B PRO O 528 206.4 119.5 61.8 59 B GLU N 529 205.3 117.7 62.5 61 B GLU CA 529 206.0 116.8 61.6 62 B GLU CB 529 205.6 115.3 61.9 63 B GLU CG 529 204.1 115.1 62.2 65 B GLU CD 529 203.8 115.1 63.7 66 B GLU OE1 529 202.9 114.3 64.0 67 B GLU OE2 529 204.4 115.8 64.5 67 B GLU C 529 205.7 117.2 60.1 61 B GLU O 529 206.5 116.9 59.2 62 B HIS N 530 204.5 117.8 59.9 61 B HIS CA 530 204.1 118.2 58.6 60 B HIS CB 530 202.7 118.8 58.6 61 B HIS CG 530 202.2 119.4 57.3 60 B HIS CD2 530 201.4 118.9 56.3 60 B HIS ND1 530 202.6 120.7 56.9 60 B HIS CE1 530 202.0 121.0 55.8 60 B HIS NE2 530 201.3 119.9 55.4 60 B HIS C 530 205.1 119.1 57.9 59 B HIS O 530 205.1 119.2 56.6 59 B ALA N 531 205.9 119.8 58.6 58 B ALA CA 531 206.8 120.7 58.0 58 B ALA CB 531 207.5 121.5 59.1 59 B ALA C 531 207.9 119.9 57.2 58 B ALA O 531 208.5 120.5 56.3 57 B ARG N 532 208.1 118.7 57.5 57 B ARG CA 532 209.0 117.8 56.8 57 B ARG CB 532 209.2 116.5 57.5 58 B ARG CG 532 210.1 116.5 58.7 60 B ARG CD 532 209.4 116.3 60.0 62 B ARG NE 532 209.2 114.9 60.3 64 B ARG CZ 532 209.0 114.4 61.6 65 B ARG NH1 532 208.9 115.2 62.6 65 B ARG NH2 532 208.9 113.1 61.8 65 B ARG C 532 208.6 117.6 55.4 56 B ARG O 532 209.4 117.4 54.5 56 B GLU N 533 207.3 117.7 55.1 54 B GLU CA 533 206.7 117.6 53.8 53 B GLU CB 533 205.2 117.3 53.9 53 B GLU CG 533 204.9 116.0 54.6 53 B GLU CD 533 205.3 114.8 53.7 54 B GLU OE1 533 204.3 114.1 53.1 54 B GLU OE2 533 206.5 114.5 53.6 54 B GLU C 533 207.0 118.8 52.9 52 B GLU O 533 206.3 119.0 51.9 52 B ARG N 534 208.0 119.5 53.2 50 B ARG CA 534 208.4 120.7 52.5 49 B ARG CB 534 209.2 121.6 53.4 50 B ARG CG 534 209.2 123.0 53.0 51 B ARG CD 534 207.9 123.6 53.6 52 B ARG NE 534 207.7 125.0 53.1 54 B ARG CZ 534 208.4 126.1 53.5 55 B ARG NH1 534 209.4 125.9 54.3 56 B ARG NH2 534 208.1 127.3 53.0 56 B ARG C 534 209.2 120.2 51.3 48 B ARG O 534 209.9 119.2 51.4 48 B LEU N 535 209.2 121.0 50.2 47 B LEU CA 535 210.0 120.7 49.0 46 B LEU CB 535 209.7 121.8 47.9 44 B LEU CG 535 210.5 121.6 46.6 43 B LEU CD1 535 209.8 120.5 45.8 43 B LEU CD2 535 210.7 122.9 45.9 43 B LEU C 535 211.5 120.6 49.2 47 B LEU O 535 212.0 121.3 50.0 47 B GLN N 536 212.1 119.6 48.5 48 B GLN CA 536 213.5 119.3 48.6 49 B GLN CB 536 213.7 117.9 49.0 50 B GLN CG 536 212.9 117.5 50.3 52 B GLN CD 536 213.5 116.4 51.0 53 B GLN OE1 536 212.9 115.5 51.6 54 B GLN NE2 536 214.9 116.5 51.1 54 B GLN C 536 214.1 119.5 47.2 50 B GLN O 536 214.2 118.5 46.5 51 B ASP N 537 214.6 120.7 47.0 51 B ASP CA 537 215.2 121.0 45.7 52 B ASP CB 537 215.3 122.5 45.5 52 B ASP CG 537 216.6 123.1 45.9 52 B ASP OD1 537 217.2 122.5 46.8 53 B ASP OD2 537 217.1 124.1 45.3 53 B ASP C 537 216.5 120.3 45.2 53 B ASP O 537 216.9 120.6 44.1 53 B ASP N 538 217.0 119.5 46.1 54 B ASP CA 538 218.3 118.8 45.7 55 B ASP CB 538 218.1 117.8 44.6 55 B ASP CG 538 217.0 116.7 44.9 56 B ASP OD1 538 216.9 116.3 46.1 56 B ASP OD2 538 216.4 116.2 43.9 56 B ASP C 538 219.5 119.7 45.4 54 B ASP O 538 220.5 119.3 44.9 54 B SER N 539 219.3 121.0 45.7 55 B SER CA 539 220.3 122.0 45.5 55 B SER CB 539 221.6 121.6 46.2 57 B SER OG 539 221.3 121.3 47.6 58 B SER C 539 220.6 122.2 44.0 55 B SER O 539 221.6 122.6 43.6 55 B VAL N 540 219.5 121.9 43.2 53 B VAL CA 540 219.5 122.0 41.8 51 B VAL CB 540 219.5 120.6 41.0 51 B VAL CG1 540 219.5 120.8 39.6 50 B VAL CG2 540 220.7 119.8 41.5 51 B VAL C 540 218.2 122.7 41.5 50 B VAL O 540 217.2 122.0 41.4 51 B GLU N 541 218.3 124.0 41.5 49 B GLU CA 541 217.0 124.7 41.3 48 B GLU CB 541 217.0 126.0 42.1 50 B GLU CG 541 218.4 126.5 42.4 53 B GLU CD 541 218.4 127.8 43.1 55 B GLU OE1 541 218.5 128.9 42.4 56 B GLU OE2 541 218.2 127.9 44.4 56 B GLU C 541 216.8 125.0 39.9 46 B GLU O 541 217.7 125.2 39.1 47 B THR N 542 215.5 125.0 39.5 43 B THR CA 542 215.0 125.3 38.1 40 B THR CB 542 214.7 124.0 37.4 40 B THR OG1 542 213.7 123.3 38.2 40 B THR CG2 542 215.9 123.1 37.4 40 B THR C 542 213.8 126.1 38.3 38 B THR O 542 213.3 126.3 39.4 38 B VAL N 543 213.3 126.7 37.2 36 B VAL CA 543 212.1 127.6 37.3 34 B VAL CB 543 211.6 127.9 36.0 33 B VAL CG1 543 210.4 128.9 36.1 33 B VAL CG2 543 212.6 128.4 35.0 33 B VAL C 543 211.0 126.9 38.1 34 B VAL O 543 210.3 127.6 38.8 35 B THR N 544 210.9 125.6 38.0 33 B THR CA 544 209.9 124.8 38.7 33 B THR CB 544 209.9 123.4 38.2 33 B THR OG1 544 209.7 123.4 36.8 32 B THR CG2 544 208.7 122.6 38.9 32 B THR C 544 210.0 124.8 40.2 33 B THR O 544 209.1 125.1 40.9 33 B SER N 545 211.2 124.4 40.8 33 B SER CA 545 211.4 124.3 42.2 32 B SER CB 545 212.7 123.6 42.5 32 B SER OG 545 213.8 124.3 41.7 31 B SER C 545 211.3 125.7 42.8 33 B SER O 545 210.7 125.9 43.9 34 B ILE N 546 211.8 126.7 42.1 33 B ILE CA 546 211.8 128.1 42.5 32 B ILE CB 546 212.4 129.0 41.4 32 B ILE CG2 546 212.2 130.4 41.8 32 B ILE CG1 546 213.9 128.7 41.4 32 B ILE CD1 546 214.6 129.4 40.2 33 B ILE C 546 210.3 128.5 42.7 32 B ILE O 546 210.0 129.0 43.8 33 B GLU N 547 209.4 128.3 41.7 32 B GLU CA 547 208.0 128.7 41.8 32 B GLU CB 547 207.3 128.6 40.5 33 B GLU CG 547 207.9 129.5 39.4 35 B GLU CD 547 208.0 131.0 39.9 37 B GLU OE1 547 207.0 131.5 40.4 37 B GLU OE2 547 209.1 131.5 39.8 38 B GLU C 547 207.3 127.9 42.8 31 B GLU O 547 206.5 128.5 43.6 31 B GLN N 548 207.4 126.6 42.8 31 B GLN CA 548 206.8 125.7 43.8 32 B GLN CB 548 207.2 124.3 43.7 30 B GLN CG 548 206.8 123.3 44.8 28 B GLN CD 548 205.3 123.2 44.9 27 B GLN OE1 548 204.8 123.2 46.1 27 B GLN NE2 548 204.6 123.2 43.8 27 B GLN C 548 207.1 126.3 45.2 33 B GLN O 548 206.3 126.5 46.1 32 B ALA N 549 208.4 126.5 45.4 34 B ALA CA 549 209.0 127.0 46.6 35 B ALA CB 549 210.5 127.2 46.5 35 B ALA C 549 208.4 128.3 47.1 35 B ALA O 549 208.4 128.6 48.2 35 B LYS N 550 208.0 129.2 46.1 36 B LYS CA 550 207.4 130.4 46.5 38 B LYS CB 550 207.2 131.3 45.2 39 B LYS CG 550 208.5 131.9 44.7 41 B LYS CD 550 208.3 132.8 43.5 42 B LYS CE 550 209.6 133.0 42.8 42 B LYS NZ 550 209.4 133.8 41.5 43 B LYS C 550 206.0 130.2 47.1 38 B LYS O 550 205.7 130.7 48.1 39 B VAL N 551 205.3 129.3 46.4 39 B VAL CA 551 203.9 128.9 46.8 39 B VAL CB 551 203.2 127.9 46.0 38 B VAL CG1 551 201.9 127.5 46.5 38 B VAL CG2 551 203.1 128.3 44.5 38 B VAL C 551 204.0 128.4 48.3 40 B VAL O 551 203.3 129.0 49.2 40 B GLU N 552 204.8 127.4 48.5 41 B GLU CA 552 204.9 126.8 49.8 42 B GLU CB 552 206.0 125.7 49.8 41 B GLU CG 552 205.7 124.5 48.9 38 B GLU CD 552 206.7 123.4 49.2 37 B GLU OE1 552 207.7 123.6 49.8 36 B GLU OE2 552 206.4 122.3 48.7 37 B GLU C 552 205.1 127.8 50.9 44 B GLU O 552 204.4 127.7 51.9 45 B GLU N 553 206.0 128.7 50.7 47 B GLU CA 553 206.3 129.7 51.6 49 B GLU CB 553 207.4 130.6 51.1 51 B GLU CG 553 207.9 131.6 52.2 55 B GLU CD 553 209.4 131.7 52.2 57 B GLU OE1 553 210.0 130.7 52.4 59 B GLU OE2 553 209.9 132.8 51.9 58 B GLU C 553 205.0 130.6 52.0 49 B GLU O 553 204.8 130.9 53.2 49 B LYS N 554 204.3 131.0 51.0 50 B LYS CA 554 203.1 131.7 51.3 52 B LYS CB 554 202.4 132.2 50.0 54 B LYS CG 554 203.3 132.8 49.0 57 B LYS CD 554 202.7 133.1 47.7 59 B LYS CE 554 203.5 133.9 46.8 61 B LYS NZ 554 202.7 134.7 45.8 63 B LYS C 554 202.1 130.9 52.0 52 B LYS O 554 201.4 131.4 52.9 51 B ILE N 555 202.0 129.6 51.7 52 B ILE CA 555 201.1 128.7 52.3 51 B ILE CB 555 201.1 127.3 51.6 50 B ILE CG2 555 200.1 126.4 52.4 50 B ILE CG1 555 200.7 127.5 50.2 50 B ILE CD1 555 199.3 128.1 49.9 50 B ILE C 555 201.5 128.5 53.7 52 B ILE O 555 200.7 128.5 54.7 51 B GLN N 556 202.8 128.4 53.9 53 B GLN CA 556 203.4 128.2 55.2 54 B GLN CB 556 204.9 128.2 55.1 55 B GLN CG 556 205.6 128.2 56.4 55 B GLN CD 556 205.4 126.9 57.1 56 B GLN OE1 556 206.3 126.0 57.2 57 B GLN NE2 556 204.2 126.7 57.7 56 B GLN C 556 202.9 129.3 56.1 55 B GLN O 556 202.2 129.1 57.1 56 B GLU N 557 203.2 130.5 55.7 56 B GLU CA 557 202.8 131.7 56.5 58 B GLU CB 557 203.1 133.0 55.7 60 B GLU CG 557 204.6 133.1 55.3 63 B GLU CD 557 205.0 134.4 54.5 65 B GLU OE1 557 204.1 135.3 54.3 65 B GLU OE2 557 206.1 134.5 53.9 65 B GLU C 557 201.3 131.7 56.9 57 B GLU O 557 201.0 132.3 57.9 57 B VAL N 558 200.5 131.1 56.1 56 B VAL CA 558 199.1 131.0 56.4 55 B VAL CB 558 198.2 130.5 55.1 55 B VAL CG1 558 196.8 130.0 55.6 55 B VAL CG2 558 198.1 131.6 54.1 55 B VAL C 558 198.8 130.0 57.5 55 B VAL O 558 198.1 130.4 58.5 55 B PHE N 559 199.5 128.9 57.5 55 B PHE CA 559 199.3 127.9 58.5 55 B PHE CB 559 200.1 126.6 58.2 54 B PHE CG 559 199.5 125.9 57.0 53 B PHE CD1 559 200.2 125.0 56.2 52 B PHE CD2 559 198.1 126.1 56.7 52 B PHE CE1 559 199.6 124.4 55.1 52 B PHE CE2 559 197.5 125.4 55.6 51 B PHE CZ 559 198.3 124.6 54.8 51 B PHE C 559 199.8 128.5 59.9 56 B PHE O 559 199.1 128.4 60.9 56 B SER N 560 201.0 129.1 59.8 58 B SER CA 560 201.5 129.7 61.0 60 B SER CB 560 203.0 130.0 60.9 59 B SER OG 560 203.7 128.8 60.6 59 B SER C 560 200.8 131.0 61.6 62 B SER O 560 201.1 131.4 62.7 63 B SER N 561 199.9 131.5 60.8 64 B SER CA 561 199.2 132.7 61.3 67 B SER CB 561 198.2 133.2 60.3 67 B SER OG 561 197.2 132.3 60.0 67 B SER C 561 198.5 132.3 62.6 69 B SER O 561 198.4 133.1 63.5 70 B TYR N 562 197.9 131.1 62.6 72 B TYR CA 562 197.2 130.5 63.7 74 B TYR CB 562 196.7 129.1 63.3 73 B TYR CG 562 195.5 129.3 62.4 73 B TYR CD1 562 195.6 128.8 61.0 73 B TYR CE1 562 194.6 129.0 60.1 73 B TYR CD2 562 194.3 129.9 62.7 73 B TYR CE2 562 193.3 130.1 61.8 73 B TYR CZ 562 193.4 129.7 60.5 73 B TYR OH 562 192.4 129.9 59.6 73 B TYR C 562 198.1 130.4 64.9 76 B TYR O 562 197.8 131.0 66.0 76 B LYS N 563 199.3 129.8 64.7 78 B LYS CA 563 200.3 129.6 65.8 80 B LYS CB 563 201.3 128.5 65.3 81 B LYS CG 563 200.9 127.1 65.7 81 B LYS CD 563 201.3 126.1 64.6 82 B LYS CE 563 202.7 126.1 64.2 82 B LYS NZ 563 203.5 124.9 64.7 82 B LYS C 563 201.0 130.9 66.0 81 B LYS O 563 202.2 130.9 66.2 81 B PHE N 564 200.3 132.0 66.1 83 B PHE CA 564 200.9 133.3 66.3 85 B PHE CB 564 200.7 134.2 65.1 88 B PHE CG 564 201.1 135.6 65.3 90 B PHE CD1 564 202.5 135.9 65.4 91 B PHE CD2 564 200.2 136.7 65.3 91 B PHE CE1 564 202.9 137.3 65.6 92 B PHE CE2 564 200.6 138.0 65.5 91 B PHE CZ 564 202.0 138.3 65.7 92 B PHE C 564 200.5 134.0 67.6 86 B PHE O 564 199.7 134.9 67.6 85 B ASN N 565 201.0 133.6 68.8 86 B ASN CA 565 200.8 134.2 70.1 85 B ASN CB 565 201.6 135.5 70.3 86 B ASN CG 565 202.9 135.2 71.0 88 B ASN OD1 565 203.1 134.1 71.5 89 B ASN ND2 565 203.7 136.3 71.2 89 B ASN C 565 199.4 134.6 70.3 84 B ASN O 565 199.1 135.4 71.1 84 B HIS N 566 198.5 134.0 69.5 84 B HIS CA 566 197.1 134.5 69.5 84 B HIS CB 566 196.7 135.0 68.1 86 B HIS CG 566 196.8 136.5 68.0 88 B HIS CD2 566 195.9 137.5 68.3 89 B HIS ND1 566 198.0 137.2 67.7 89 B HIS CE1 566 197.8 138.5 67.8 90 B HIS NE2 566 196.5 138.7 68.2 90 B HIS C 566 196.0 133.6 70.0 82 B HIS O 566 195.9 133.4 71.2 81 B LEU N 567 195.2 133.2 69.1 81 B LEU CA 567 194.0 132.4 69.4 80 B LEU CB 567 192.7 133.0 68.7 80 B LEU CG 567 192.8 134.1 67.7 80 B LEU CD1 567 193.3 135.4 68.4 80 B LEU CD2 567 193.7 133.8 66.5 80 B LEU C 567 194.3 131.0 68.9 80 B LEU O 567 195.4 130.7 68.4 80 B VAL N 568 193.2 130.2 68.9 79 B VAL CA 568 193.2 128.8 68.5 77 B VAL CB 568 192.4 127.9 69.4 77 B VAL CG1 568 192.7 126.4 69.2 77 B VAL CG2 568 192.7 128.2 70.9 76 B VAL C 568 192.7 128.7 67.0 76 B VAL O 568 191.8 129.5 66.7 76 B PRO N 569 193.2 127.9 66.1 75 B PRO CD 569 194.4 127.0 66.2 74 B PRO CA 569 192.7 127.9 64.8 74 B PRO CB 569 193.5 126.8 64.1 74 B PRO CG 569 194.0 125.9 65.2 74 B PRO C 569 191.2 127.5 64.7 73 B PRO O 569 190.7 126.5 65.2 73 B ARG N 570 190.4 128.5 64.2 72 B ARG CA 570 189.0 128.3 64.0 71 B ARG CB 570 188.3 129.6 64.5 73 B ARG CG 570 188.1 129.8 66.0 76 B ARG CD 570 186.8 129.2 66.4 78 B ARG NE 570 186.8 127.7 66.3 79 B ARG CZ 570 186.1 126.9 67.1 81 B ARG NH1 570 185.4 127.5 68.1 81 B ARG NH2 570 186.1 125.6 67.0 82 B ARG C 570 188.6 128.1 62.6 69 B ARG O 570 188.3 129.1 61.9 70 B LEU N 571 188.7 126.9 62.1 66 B LEU CA 571 188.4 126.7 60.7 62 B LEU CB 571 188.8 125.3 60.2 62 B LEU CG 571 190.1 125.3 59.3 62 B LEU CD1 571 191.3 125.8 60.1 61 B LEU CD2 571 190.4 123.9 58.8 62 B LEU C 571 186.9 126.9 60.5 60 B LEU O 571 186.0 126.2 61.0 59 B VAL N 572 186.5 127.9 59.7 57 B VAL CA 572 185.2 128.2 59.4 55 B VAL CB 572 184.7 129.4 60.3 56 B VAL CG1 572 183.3 129.8 60.1 56 B VAL CG2 572 185.0 129.1 61.8 56 B VAL C 572 185.0 128.7 58.0 54 B VAL O 572 185.8 129.3 57.4 55 B LEU N 573 183.8 128.3 57.4 52 B LEU CA 573 183.6 128.6 56.0 50 B LEU CB 573 182.9 127.4 55.2 48 B LEU CG 573 182.3 127.8 53.9 46 B LEU CD1 573 183.4 127.8 52.9 46 B LEU CD2 573 181.2 126.9 53.5 46 B LEU C 573 182.6 129.8 56.0 49 B LEU O 573 181.4 129.7 56.2 49 B GLN N 574 183.1 131.0 55.6 49 B GLN CA 574 182.4 132.2 55.5 49 B GLN CB 574 183.2 133.4 54.9 50 B GLN CG 574 184.5 133.5 55.7 51 B GLN CD 574 184.4 133.4 57.2 52 B GLN OE1 574 185.1 132.7 57.8 54 B GLN NE2 574 183.4 134.2 57.7 52 B GLN C 574 181.1 132.1 54.6 49 B GLN O 574 181.0 132.9 53.6 50 B ARG N 575 180.1 131.4 55.0 48 B ARG CA 575 178.9 131.2 54.2 49 B ARG CB 575 177.9 130.3 55.0 49 B ARG CG 575 178.5 129.1 55.6 50 B ARG CD 575 177.5 128.4 56.5 50 B ARG NE 575 177.5 126.9 56.2 50 B ARG CZ 575 176.9 126.4 55.2 50 B ARG NH1 575 176.1 127.1 54.4 49 B ARG NH2 575 177.0 125.1 55.0 50 B ARG C 575 178.2 132.5 53.8 49 B ARG O 575 177.7 132.6 52.7 48 B GLU N 576 178.0 133.4 54.8 50 B GLU CA 576 177.3 134.6 54.5 51 B GLU CB 576 177.0 135.4 55.9 53 B GLU CG 576 176.8 134.5 57.1 55 B GLU CD 576 175.9 133.3 57.0 57 B GLU OE1 576 174.8 133.5 56.4 57 B GLU OE2 576 176.2 132.2 57.4 57 B GLU C 576 178.0 135.4 53.6 50 B GLU O 576 177.5 136.0 52.6 50 B LYS N 577 179.3 135.5 53.8 48 B LYS CA 577 180.2 136.3 52.9 46 B LYS CB 577 181.6 136.3 53.4 47 B LYS CG 577 182.0 137.7 53.9 48 B LYS CD 577 181.0 138.2 55.0 49 B LYS CE 577 180.7 139.7 54.8 49 B LYS NZ 577 179.7 140.0 53.7 50 B LYS C 577 180.1 135.8 51.4 44 B LYS O 577 179.7 136.5 50.5 43 B HIS N 578 180.2 134.4 51.3 41 B HIS CA 578 180.1 133.8 49.9 39 B HIS CB 578 180.4 132.3 50.0 36 B HIS CG 578 181.7 132.0 50.6 34 B HIS CD2 578 182.1 130.8 51.3 34 B HIS ND1 578 182.8 132.8 50.7 34 B HIS CE1 578 183.8 132.2 51.4 34 B HIS NE2 578 183.3 131.0 51.7 33 B HIS C 578 178.7 134.0 49.4 39 B HIS O 578 178.5 134.1 48.2 39 B PHE N 579 177.7 134.0 50.3 39 B PHE CA 579 176.3 134.0 49.9 40 B PHE CB 579 175.4 133.9 51.1 40 B PHE CG 579 174.0 134.1 50.8 39 B PHE CD1 579 173.3 133.2 50.0 39 B PHE CD2 579 173.3 135.3 51.1 40 B PHE CE1 579 172.0 133.5 49.5 39 B PHE CE2 579 172.0 135.6 50.7 40 B PHE CZ 579 171.4 134.7 49.9 40 B PHE C 579 176.0 135.3 49.3 41 B PHE O 579 175.4 135.4 48.2 41 B HIS N 580 176.3 136.4 49.9 44 B HIS CA 580 176.1 137.8 49.4 46 B HIS CB 580 176.4 138.8 50.5 49 B HIS CG 580 175.9 138.5 51.8 53 B HIS CD2 580 174.6 138.2 52.2 54 B HIS ND1 580 176.7 138.3 52.9 54 B HIS CE1 580 175.9 138.0 54.0 54 B HIS NE2 580 174.7 137.9 53.6 54 B HIS C 580 176.8 138.0 48.1 45 B HIS O 580 176.4 138.8 47.2 45 B TYR N 581 178.0 137.4 48.0 44 B TYR CA 581 178.9 137.5 46.9 43 B TYR CB 581 180.2 136.8 47.2 43 B TYR CG 581 181.1 136.7 46.0 44 B TYR CD1 581 181.3 137.8 45.1 44 B TYR CE1 581 182.2 137.6 44.1 44 B TYR CD2 581 181.8 135.5 45.7 44 B TYR CE2 581 182.6 135.3 44.7 44 B TYR CZ 581 182.8 136.4 43.8 44 B TYR OH 581 183.7 136.3 42.8 45 B TYR C 581 178.2 136.9 45.7 43 B TYR O 581 178.0 137.5 44.6 42 B LEU N 582 177.8 135.6 45.8 42 B LEU CA 582 177.2 134.8 44.8 41 B LEU CB 582 177.0 133.4 45.3 39 B LEU CG 582 178.2 132.6 45.4 37 B LEU CD1 582 178.1 131.7 46.6 36 B LEU CD2 582 178.5 131.8 44.2 37 B LEU C 582 175.8 135.4 44.5 43 B LEU O 582 175.4 135.5 43.3 43 B LYS N 583 175.2 135.9 45.5 45 B LYS CA 583 173.9 136.5 45.5 48 B LYS CB 583 173.4 136.9 46.9 50 B LYS CG 583 172.0 137.5 47.0 52 B LYS CD 583 171.8 138.2 48.4 54 B LYS CE 583 170.8 139.4 48.3 55 B LYS NZ 583 169.3 139.1 48.0 55 B LYS C 583 173.8 137.7 44.5 49 B LYS O 583 172.8 137.8 43.8 49 B ARG N 584 174.8 138.6 44.5 50 B ARG CA 584 174.7 139.8 43.7 51 B ARG CB 584 175.4 141.1 44.2 53 B ARG CG 584 174.7 142.4 43.7 57 B ARG CD 584 175.6 143.6 43.8 59 B ARG NE 584 176.3 143.8 42.5 62 B ARG CZ 584 177.5 144.5 42.3 63 B ARG NH1 584 178.0 145.1 43.4 64 B ARG NH2 584 178.0 144.7 41.1 63 B ARG C 584 175.3 139.6 42.3 50 B ARG O 584 174.9 140.2 41.3 49 B GLY N 585 176.3 138.6 42.2 48 B GLY CA 585 176.9 138.3 40.9 47 B GLY C 585 175.9 137.6 40.1 46 B GLY O 585 176.0 137.6 38.8 45 B LEU N 586 174.9 137.0 40.7 45 B LEU CA 586 173.8 136.3 39.9 44 B LEU CB 586 173.0 135.4 40.8 45 B LEU CG 586 171.9 134.5 40.2 45 B LEU CD1 586 172.5 133.4 39.3 45 B LEU CD2 586 171.1 133.8 41.3 45 B LEU C 586 173.0 137.3 39.2 44 B LEU O 586 172.3 137.0 38.2 43 B ARG N 587 173.1 138.6 39.6 44 B ARG CA 587 172.4 139.7 39.0 45 B ARG CB 587 171.6 140.5 40.1 46 B ARG CG 587 170.1 140.4 40.0 48 B ARG CD 587 169.6 138.9 40.2 49 B ARG NE 587 168.2 138.8 40.5 50 B ARG CZ 587 167.3 138.9 39.5 51 B ARG NH1 587 167.6 139.0 38.2 51 B ARG NH2 587 166.0 138.8 39.8 51 B ARG C 587 173.2 140.6 38.1 44 B ARG O 587 172.8 141.0 37.0 43 B GLN N 588 174.4 141.0 38.6 43 B GLN CA 588 175.2 141.9 37.8 43 B GLN CB 588 174.8 143.3 37.9 46 B GLN CG 588 174.8 143.8 39.3 49 B GLN CD 588 174.7 145.3 39.4 50 B GLN OE1 588 174.4 145.9 38.3 51 B GLN NE2 588 174.9 145.9 40.5 51 B GLN C 588 176.7 141.8 38.2 41 B GLN O 588 177.1 141.6 39.4 40 B LEU N 589 177.6 142.0 37.2 38 B LEU CA 589 179.0 142.0 37.4 36 B LEU CB 589 179.5 140.7 36.7 34 B LEU CG 589 178.9 139.4 37.1 32 B LEU CD1 589 178.7 138.6 35.8 31 B LEU CD2 589 179.8 138.6 38.1 31 B LEU C 589 179.6 143.2 36.7 35 B LEU O 589 179.2 143.6 35.6 34 B THR N 590 180.8 143.6 37.2 35 B THR CA 590 181.6 144.7 36.7 36 B THR CB 590 182.7 145.0 37.7 36 B THR OG1 590 183.6 143.8 37.9 37 B THR CG2 590 182.1 145.4 39.0 37 B THR C 590 182.3 144.3 35.4 35 B THR O 590 182.4 143.1 35.1 35 B ASP N 591 182.7 145.3 34.6 35 B ASP CA 591 183.3 145.1 33.3 35 B ASP CB 591 183.6 146.4 32.6 35 B ASP CG 591 184.5 147.3 33.4 37 B ASP OD1 591 184.7 148.5 32.9 37 B ASP OD2 591 185.1 146.9 34.5 36 B ASP C 591 184.6 144.2 33.4 34 B ASP O 591 185.1 143.9 32.4 35 B ALA N 592 185.0 143.9 34.6 32 B ALA CA 592 186.2 143.0 34.8 31 B ALA CB 592 186.6 143.0 36.2 32 B ALA C 592 185.8 141.6 34.4 30 B ALA O 592 186.6 140.7 34.5 29 B TYR N 593 184.5 141.4 33.9 29 B TYR CA 593 184.0 140.2 33.4 28 B TYR CB 593 182.7 139.8 34.1 27 B TYR CG 593 182.9 139.1 35.4 27 B TYR CD1 593 183.0 139.7 36.6 27 B TYR CE1 593 183.4 139.0 37.8 27 B TYR CD2 593 183.3 137.7 35.4 27 B TYR CE2 593 183.6 137.0 36.5 26 B TYR CZ 593 183.7 137.7 37.7 26 B TYR OH 593 184.1 137.0 38.8 27 B TYR C 593 183.7 140.2 31.9 29 B TYR O 593 183.0 139.3 31.4 29 B GLU N 594 184.2 141.3 31.3 28 B GLU CA 594 184.0 141.4 29.9 28 B GLU CB 594 184.6 142.6 29.3 30 B GLU CG 594 183.9 143.9 29.7 32 B GLU CD 594 184.6 145.1 29.4 33 B GLU OE1 594 184.0 146.1 28.9 34 B GLU OE2 594 185.9 145.1 29.5 34 B GLU C 594 184.6 140.2 29.2 27 B GLU O 594 184.2 139.8 28.1 27 B CYS N 595 185.6 139.6 29.8 26 B CYS CA 595 186.3 138.4 29.3 24 B CYS CB 595 187.6 138.1 30.0 22 B CYS SG 595 187.6 137.9 31.8 19 B CYS C 595 185.4 137.2 29.3 24 B CYS O 595 185.4 136.3 28.4 24 B LEU N 596 184.6 137.1 30.4 22 B LEU CA 596 183.6 136.0 30.5 20 B LEU CB 596 183.4 135.6 31.9 20 B LEU CG 596 184.5 134.6 32.4 20 B LEU CD1 596 184.7 134.7 33.9 20 B LEU CD2 596 184.2 133.2 31.9 20 B LEU C 596 182.3 136.4 29.8 20 B LEU O 596 181.3 135.7 29.9 19 B ASP N 597 182.3 137.4 29.0 21 B ASP CA 597 181.1 137.8 28.2 21 B ASP CB 597 181.4 139.2 27.5 20 B ASP CG 597 180.3 139.5 26.6 19 B ASP OD1 597 179.1 139.6 27.0 19 B ASP OD2 597 180.6 139.8 25.4 20 B ASP C 597 180.7 136.8 27.2 23 B ASP O 597 179.7 137.0 26.5 25 B ALA N 598 181.4 135.7 27.0 24 B ALA CA 598 181.0 134.6 26.1 24 B ALA CB 598 181.9 134.5 24.9 24 B ALA C 598 180.9 133.3 26.8 25 B ALA O 598 180.7 132.2 26.2 25 B SER N 599 180.9 133.3 28.1 26 B SER CA 599 180.8 132.2 29.0 27 B SER CB 599 182.1 131.9 29.7 27 B SER OG 599 183.2 131.7 28.8 28 B SER C 599 179.7 132.5 30.1 27 B SER O 599 179.9 132.2 31.2 27 B ARG N 600 178.6 133.1 29.6 27 B ARG CA 600 177.6 133.5 30.6 27 B ARG CB 600 176.7 134.6 30.1 27 B ARG CG 600 177.5 135.9 29.9 28 B ARG CD 600 176.7 137.0 29.3 29 B ARG NE 600 175.8 137.6 30.3 30 B ARG CZ 600 174.8 138.4 30.1 31 B ARG NH1 600 174.6 138.7 28.8 31 B ARG NH2 600 174.0 138.9 31.0 32 B ARG C 600 176.8 132.3 31.2 27 B ARG O 600 176.6 132.3 32.4 29 B PRO N 601 176.5 131.3 30.4 25 B PRO CD 601 176.4 131.1 29.0 26 B PRO CA 601 175.8 130.2 31.1 24 B PRO CB 601 175.5 129.2 30.0 24 B PRO CG 601 175.3 130.1 28.8 24 B PRO C 601 176.7 129.7 32.2 24 B PRO O 601 176.2 129.2 33.2 25 B TRP N 602 178.0 129.7 32.0 23 B TRP CA 602 178.8 129.2 33.1 23 B TRP CB 602 180.3 129.3 32.7 23 B TRP CG 602 180.7 128.3 31.8 23 B TRP CD2 602 181.1 126.9 32.1 23 B TRP CE2 602 181.5 126.3 30.9 23 B TRP CE3 602 181.0 126.1 33.3 23 B TRP CD1 602 181.0 128.4 30.4 23 B TRP NE1 602 181.5 127.2 29.9 23 B TRP CZ2 602 181.9 124.9 30.9 23 B TRP CZ3 602 181.4 124.8 33.2 22 B TRP CH2 602 181.8 124.2 32.1 22 B TRP C 602 178.6 130.1 34.3 24 B TRP O 602 178.3 129.5 35.4 24 B LEU N 603 178.6 131.4 34.1 25 B LEU CA 603 178.3 132.3 35.2 26 B LEU CB 603 178.3 133.7 34.7 26 B LEU CG 603 179.7 134.3 34.4 27 B LEU CD1 603 179.7 135.6 33.6 26 B LEU CD2 603 180.4 134.5 35.7 26 B LEU C 603 177.1 131.9 36.0 27 B LEU O 603 177.1 132.1 37.2 28 B CYS N 604 176.0 131.5 35.3 26 B CYS CA 604 174.8 131.0 36.0 25 B CYS CB 604 173.7 130.8 35.0 25 B CYS SG 604 173.2 132.2 34.1 28 B CYS C 604 175.2 129.8 36.7 25 B CYS O 604 175.2 129.8 38.0 25 B TYR N 605 175.5 128.7 36.0 24 B TYR CA 605 175.9 127.4 36.6 22 B TYR CB 605 176.5 126.5 35.6 21 B TYR CG 605 177.1 125.2 36.3 21 B TYR CD1 605 176.4 124.3 37.0 21 B TYR CE1 605 177.0 123.2 37.6 20 B TYR CD2 605 178.5 125.1 36.3 21 B TYR CE2 605 179.1 124.0 36.9 21 B TYR CZ 605 178.4 123.1 37.6 21 B TYR OH 605 179.0 122.1 38.2 22 B TYR C 605 176.8 127.6 37.8 23 B TYR O 605 176.5 127.2 39.0 22 B TRP N 606 178.0 128.2 37.6 24 B TRP CA 606 178.9 128.4 38.7 25 B TRP CB 606 180.1 129.3 38.2 26 B TRP CG 606 181.1 128.7 37.2 27 B TRP CD2 606 181.8 129.5 36.2 28 B TRP CE2 606 182.6 128.6 35.6 27 B TRP CE3 606 181.8 130.8 35.9 29 B TRP CD1 606 181.5 127.4 37.1 26 B TRP NE1 606 182.4 127.3 36.1 26 B TRP CZ2 606 183.5 129.0 34.5 28 B TRP CZ3 606 182.6 131.2 34.8 29 B TRP CH2 606 183.5 130.3 34.2 28 B TRP C 606 178.3 128.9 39.9 26 B TRP O 606 178.5 128.5 41.0 26 B ILE N 607 177.5 130.0 39.7 27 B ILE CA 607 176.8 130.6 40.9 28 B ILE CB 607 176.4 132.1 40.5 27 B ILE CG2 607 175.6 132.7 41.7 27 B ILE CG1 607 177.6 132.9 40.2 26 B ILE CD1 607 177.3 134.2 39.4 26 B ILE C 607 175.7 129.8 41.4 28 B ILE O 607 175.7 129.4 42.6 29 B LEU N 608 174.7 129.6 40.6 28 B LEU CA 608 173.5 128.8 40.9 28 B LEU CB 608 172.7 128.5 39.7 27 B LEU CG 608 171.2 128.9 39.7 27 B LEU CD1 608 170.9 130.2 40.4 27 B LEU CD2 608 170.7 128.9 38.2 27 B LEU C 608 173.9 127.5 41.6 28 B LEU O 608 173.2 126.9 42.4 30 B HIS N 609 175.1 126.9 41.2 28 B HIS CA 609 175.6 125.7 41.8 29 B HIS CB 609 176.5 124.9 40.9 28 B HIS CG 609 177.1 123.7 41.5 28 B HIS CD2 609 178.4 123.3 41.8 28 B HIS ND1 609 176.4 122.7 42.0 27 B HIS CE1 609 177.1 121.7 42.6 27 B HIS NE2 609 178.4 122.1 42.4 28 B HIS C 609 176.2 125.9 43.2 30 B HIS O 609 176.0 125.1 44.1 30 B SER N 610 176.9 127.0 43.4 32 B SER CA 610 177.6 127.3 44.6 33 B SER CB 610 178.5 128.5 44.5 34 B SER OG 610 179.4 128.4 43.4 34 B SER C 610 176.5 127.5 45.7 34 B SER O 610 176.7 127.1 46.9 33 B LEU N 611 175.5 128.2 45.4 35 B LEU CA 611 174.4 128.5 46.3 35 B LEU CB 611 173.3 129.3 45.6 34 B LEU CG 611 173.6 130.7 45.0 34 B LEU CD1 611 172.4 131.4 44.4 33 B LEU CD2 611 174.2 131.6 46.1 33 B LEU C 611 173.8 127.1 46.6 36 B LEU O 611 173.7 126.8 47.8 38 B GLU N 612 173.5 126.3 45.6 37 B GLU CA 612 173.1 125.0 45.8 37 B GLU CB 612 173.0 124.2 44.5 37 B GLU CG 612 172.5 122.8 44.6 37 B GLU CD 612 173.3 121.9 43.7 37 B GLU OE1 612 173.8 120.9 44.2 37 B GLU OE2 612 173.3 122.1 42.4 36 B GLU C 612 173.9 124.2 46.8 38 B GLU O 612 173.4 123.6 47.7 38 B LEU N 613 175.2 124.4 46.8 39 B LEU CA 613 176.1 123.7 47.7 41 B LEU CB 613 177.6 123.8 47.2 40 B LEU CG 613 178.0 122.9 46.0 40 B LEU CD1 613 179.1 123.6 45.2 40 B LEU CD2 613 178.5 121.6 46.6 41 B LEU C 613 176.0 124.3 49.1 42 B LEU O 613 175.8 123.6 50.1 42 B LEU N 614 176.0 125.6 49.2 44 B LEU CA 614 175.9 126.3 50.5 46 B LEU CB 614 176.2 127.8 50.3 45 B LEU CG 614 177.5 128.2 49.8 44 B LEU CD1 614 177.4 129.4 49.0 44 B LEU CD2 614 178.5 128.3 50.9 45 B LEU C 614 174.6 126.1 51.1 47 B LEU O 614 174.3 126.4 52.3 47 B ASP N 615 173.6 125.6 50.3 50 B ASP CA 615 172.3 125.3 50.7 52 B ASP CB 615 172.2 124.6 52.0 52 B ASP CG 615 170.8 124.0 52.3 53 B ASP OD1 615 169.9 124.0 51.4 53 B ASP OD2 615 170.7 123.5 53.4 52 B ASP C 615 171.4 126.6 50.7 53 B ASP O 615 170.6 126.7 51.5 55 B GLU N 616 171.8 127.5 49.8 55 B GLU CA 616 171.0 128.7 49.7 56 B GLU CB 616 171.9 129.9 49.4 58 B GLU CG 616 173.2 129.9 50.3 60 B GLU CD 616 172.9 130.4 51.7 61 B GLU OE1 616 171.7 130.6 52.1 62 B GLU OE2 616 173.9 130.5 52.5 62 B GLU C 616 169.9 128.5 48.7 57 B GLU O 616 170.1 127.7 47.8 57 B PRO N 617 168.8 129.2 48.8 58 B PRO CD 617 168.6 130.3 49.7 59 B PRO CA 617 167.7 129.1 47.8 59 B PRO CB 617 166.6 129.9 48.6 59 B PRO CG 617 167.4 131.1 49.1 59 B PRO C 617 167.9 129.8 46.5 59 B PRO O 617 168.7 130.8 46.4 59 B ILE N 618 167.2 129.3 45.5 60 B ILE CA 618 167.3 129.9 44.1 61 B ILE CB 618 167.8 128.8 43.1 61 B ILE CG2 618 167.6 129.1 41.7 60 B ILE CG1 618 169.3 128.5 43.3 61 B ILE CD1 618 169.8 127.9 44.6 60 B ILE C 618 165.8 130.3 43.8 60 B ILE O 618 165.1 129.6 43.1 61 B PRO N 619 165.4 131.4 44.4 60 B PRO CD 619 166.3 132.3 45.2 60 B PRO CA 619 164.1 132.1 44.3 59 B PRO CB 619 164.4 133.5 44.5 59 B PRO CG 619 165.3 133.5 45.6 59 B PRO C 619 163.3 131.8 43.0 58 B PRO O 619 163.8 132.0 41.9 58 B GLN N 620 162.0 131.6 43.2 58 B GLN CA 620 161.1 131.3 42.1 59 B GLN CB 620 159.7 131.1 42.6 60 B GLN CG 620 159.6 130.4 44.1 62 B GLN CD 620 158.5 129.5 44.3 63 B GLN OE1 620 157.4 129.6 43.6 64 B GLN NE2 620 158.6 128.6 45.3 63 B GLN C 620 161.2 132.3 41.0 57 B GLN O 620 160.9 131.9 39.8 57 B ILE N 621 161.6 133.5 41.3 56 B ILE CA 621 161.7 134.6 40.3 56 B ILE CB 621 161.3 136.0 40.9 56 B ILE CG2 621 161.2 137.0 39.8 55 B ILE CG1 621 160.0 135.9 41.7 57 B ILE CD1 621 160.2 135.2 43.1 57 B ILE C 621 163.0 134.7 39.6 54 B ILE O 621 163.1 134.8 38.4 53 B VAL N 622 164.1 134.6 40.4 52 B VAL CA 622 165.4 134.7 39.8 51 B VAL CB 622 166.5 134.6 40.9 51 B VAL CG1 622 166.7 133.2 41.5 50 B VAL CG2 622 167.8 135.2 40.4 51 B VAL C 622 165.6 133.5 38.9 51 B VAL O 622 166.2 133.5 37.8 50 B ALA N 623 164.9 132.4 39.3 51 B ALA CA 623 164.9 131.1 38.5 50 B ALA CB 623 164.1 130.0 39.3 49 B ALA C 623 164.2 131.3 37.2 49 B ALA O 623 164.8 130.9 36.2 50 B THR N 624 163.1 132.0 37.1 48 B THR CA 624 162.4 132.2 35.8 47 B THR CB 624 161.1 133.0 36.0 46 B THR OG1 624 160.3 132.2 36.8 47 B THR CG2 624 160.4 133.2 34.6 45 B THR C 624 163.3 133.1 34.9 48 B THR O 624 163.4 132.9 33.7 47 B ASP N 625 164.0 134.0 35.5 48 B ASP CA 625 164.9 134.9 34.8 47 B ASP CB 625 165.4 136.0 35.7 49 B ASP CG 625 164.3 136.9 36.3 50 B ASP OD1 625 163.3 137.2 35.6 50 B ASP OD2 625 164.4 137.3 37.5 50 B ASP C 625 166.1 134.1 34.2 45 B ASP O 625 166.3 134.2 33.0 45 B VAL N 626 166.7 133.3 35.1 43 B VAL CA 626 167.8 132.4 34.6 42 B VAL CB 626 168.2 131.5 35.7 42 B VAL CG1 626 169.2 130.5 35.1 42 B VAL CG2 626 168.8 132.2 36.9 42 B VAL C 626 167.2 131.7 33.4 42 B VAL O 626 167.8 131.6 32.4 43 B CYS N 627 166.0 131.1 33.6 43 B CYS CA 627 165.4 130.3 32.5 43 B CYS CB 627 164.1 129.7 32.9 42 B CYS SG 627 164.2 128.4 34.1 43 B CYS C 627 165.2 131.1 31.2 44 B CYS O 627 165.8 130.8 30.2 44 B GLN N 628 164.5 132.2 31.3 44 B GLN CA 628 164.2 133.1 30.2 43 B GLN CB 628 163.4 134.3 30.7 46 B GLN CG 628 161.9 134.1 30.8 47 B GLN CD 628 161.2 135.4 31.3 48 B GLN OE1 628 161.5 136.6 31.0 48 B GLN NE2 628 160.2 135.2 32.2 49 B GLN C 628 165.5 133.5 29.6 42 B GLN O 628 165.5 133.7 28.3 41 B PHE N 629 166.6 133.7 30.4 40 B PHE CA 629 167.9 134.1 29.8 39 B PHE CB 629 168.8 134.6 31.0 38 B PHE CG 629 170.2 135.0 30.5 38 B PHE CD1 629 170.4 136.0 29.6 38 B PHE CD2 629 171.3 134.2 30.9 38 B PHE CE1 629 171.6 136.3 29.1 38 B PHE CE2 629 172.6 134.5 30.4 37 B PHE CZ 629 172.7 135.6 29.5 37 B PHE C 629 168.6 133.0 29.0 38 B PHE O 629 169.0 133.2 27.9 37 B LEU N 630 168.6 131.8 29.6 36 B LEU CA 630 169.2 130.7 29.0 35 B LEU CB 630 169.3 129.5 29.9 32 B LEU CG 630 170.2 129.7 31.1 31 B LEU CD1 630 170.1 128.7 32.2 30 B LEU CD2 630 171.6 129.8 30.6 30 B LEU C 630 168.5 130.3 27.7 37 B LEU O 630 169.0 129.7 26.7 37 B GLU N 631 167.2 130.8 27.6 38 B GLU CA 631 166.4 130.7 26.4 40 B GLU CB 631 165.0 131.0 26.7 43 B GLU CG 631 164.2 130.0 27.6 46 B GLU CD 631 162.7 130.3 27.6 49 B GLU OE1 631 162.2 130.7 28.7 50 B GLU OE2 631 162.1 130.1 26.6 50 B GLU C 631 167.0 131.6 25.3 39 B GLU O 631 166.8 131.4 24.1 39 B LEU N 632 167.5 132.7 25.8 39 B LEU CA 632 168.0 133.8 24.9 39 B LEU CB 632 168.1 135.1 25.6 39 B LEU CG 632 166.8 135.8 25.7 39 B LEU CD1 632 166.9 137.0 26.7 39 B LEU CD2 632 166.4 136.3 24.4 38 B LEU C 632 169.3 133.3 24.3 38 B LEU O 632 169.7 133.6 23.2 39 B CYS N 633 170.1 132.6 25.2 38 B CYS CA 633 171.4 132.1 24.7 37 B CYS CB 633 172.2 131.6 25.9 36 B CYS SG 633 172.6 132.9 27.0 36 B CYS C 633 171.2 130.9 23.7 37 B CYS O 633 171.9 130.8 22.7 36 B GLN N 634 170.2 130.0 24.0 37 B GLN CA 634 169.9 128.9 23.2 37 B GLN CB 634 168.6 128.2 23.7 36 B GLN CG 634 168.2 127.0 22.9 36 B GLN CD 634 167.3 126.1 23.8 36 B GLN OE1 634 166.2 126.5 24.2 37 B GLN NE2 634 167.7 124.9 24.0 36 B GLN C 634 169.8 129.2 21.7 37 B GLN O 634 169.1 130.1 21.3 37 B SER N 635 170.5 128.3 20.9 37 B SER CA 635 170.5 128.5 19.5 38 B SER CB 635 171.8 127.9 18.9 38 B SER OG 635 171.7 127.6 17.5 38 B SER C 635 169.4 127.9 18.8 39 B SER O 635 168.7 126.9 19.3 40 B PRO N 636 169.0 128.4 17.7 39 B PRO CD 636 169.4 129.7 17.1 39 B PRO CA 636 167.9 127.9 16.9 40 B PRO CB 636 167.5 129.0 15.9 40 B PRO CG 636 168.9 129.7 15.7 40 B PRO C 636 168.4 126.6 16.1 40 B PRO O 636 167.8 126.3 15.1 39 B ASP N 637 169.5 126.1 16.5 40 B ASP CA 637 170.1 124.9 15.9 41 B ASP CB 637 171.3 125.3 15.1 43 B ASP CG 637 170.9 126.2 13.9 46 B ASP OD1 637 169.8 126.0 13.3 47 B ASP OD2 637 171.6 127.2 13.6 48 B ASP C 637 170.6 124.0 17.0 39 B ASP O 637 171.6 123.3 16.8 39 B GLY N 638 169.9 124.1 18.2 37 B GLY CA 638 170.2 123.3 19.3 34 B GLY C 638 171.5 123.8 20.0 33 B GLY O 638 172.2 124.5 19.4 33 B GLY N 639 171.6 123.4 21.3 32 B GLY CA 639 172.8 123.9 22.0 32 B GLY C 639 172.7 125.4 22.4 32 B GLY O 639 171.9 126.1 21.8 32 B PHE N 640 173.5 125.8 23.3 31 B PHE CA 640 173.5 127.2 23.8 31 B PHE CB 640 173.3 127.1 25.3 32 B PHE CG 640 172.0 126.5 25.7 32 B PHE CD1 640 172.0 125.1 25.8 33 B PHE CD2 640 170.9 127.2 26.1 33 B PHE CE1 640 170.8 124.4 26.2 33 B PHE CE2 640 169.7 126.6 26.5 33 B PHE CZ 640 169.7 125.2 26.5 34 B PHE C 640 174.7 128.0 23.4 30 B PHE O 640 175.8 127.5 23.2 31 B GLY N 641 174.5 129.3 23.2 28 B GLY CA 641 175.6 130.2 22.8 26 B GLY C 641 176.1 130.7 24.2 25 B GLY O 641 175.5 130.4 25.2 25 B GLY N 642 177.3 131.4 24.1 24 B GLY CA 642 177.8 131.9 25.4 24 B GLY C 642 177.2 133.1 26.0 24 B GLY O 642 177.6 133.6 27.1 25 B GLY N 643 176.2 133.6 25.3 23 B GLY CA 643 175.4 134.8 25.7 22 B GLY C 643 174.4 135.0 24.7 23 B GLY O 643 174.5 134.4 23.6 23 B PRO N 644 173.3 135.8 24.9 23 B PRO CD 644 173.1 136.7 26.1 23 B PRO CA 644 172.2 136.0 24.0 23 B PRO CB 644 171.5 137.3 24.5 22 B PRO CG 644 171.7 137.1 26.0 22 B PRO C 644 172.8 136.3 22.6 24 B PRO O 644 173.6 137.2 22.4 26 B GLY N 645 172.3 135.5 21.6 26 B GLY CA 645 172.8 135.7 20.3 28 B GLY C 645 174.0 135.0 19.8 28 B GLY O 645 174.3 135.0 18.6 29 B GLN N 646 174.8 134.3 20.7 28 B GLN CA 646 176.0 133.7 20.2 29 B GLN CB 646 177.0 133.6 21.4 29 B GLN CG 646 177.5 135.0 21.7 29 B GLN CD 646 178.1 135.1 23.1 29 B GLN OE1 646 177.7 135.9 23.9 30 B GLN NE2 646 178.9 134.1 23.5 30 B GLN C 646 175.8 132.3 19.6 28 B GLN O 646 174.8 131.6 20.0 29 B TYR N 647 176.6 131.9 18.7 27 B TYR CA 647 176.6 130.6 18.1 26 B TYR CB 647 177.7 130.4 17.1 25 B TYR CG 647 177.7 131.4 15.9 24 B TYR CD1 647 178.7 131.4 15.0 25 B TYR CE1 647 178.7 132.2 13.9 25 B TYR CD2 647 176.5 132.1 15.6 24 B TYR CE2 647 176.5 132.9 14.5 24 B TYR CZ 647 177.6 132.9 13.6 25 B TYR OH 647 177.5 133.6 12.4 26 B TYR C 647 176.7 129.6 19.2 26 B TYR O 647 177.5 129.8 20.1 26 B PRO N 648 176.1 128.4 19.1 25 B PRO CD 648 175.4 127.9 17.9 26 B PRO CA 648 176.2 127.4 20.1 25 B PRO CB 648 175.1 126.4 19.7 25 B PRO CG 648 175.3 126.4 18.2 26 B PRO C 648 177.5 126.8 20.3 24 B PRO O 648 178.3 126.6 19.3 24 B HIS N 649 177.9 126.4 21.5 22 B HIS CA 649 179.2 125.9 21.8 21 B HIS CB 649 180.0 127.1 22.1 21 B HIS CG 649 181.5 126.7 22.4 20 B HIS CD2 649 182.6 127.1 21.8 20 B HIS ND1 649 181.9 126.1 23.6 20 B HIS CE1 649 183.2 126.1 23.6 20 B HIS NE2 649 183.7 126.6 22.5 20 B HIS C 649 179.0 124.9 22.9 22 B HIS O 649 178.3 125.3 23.9 23 B LEU N 650 179.5 123.7 22.8 21 B LEU CA 650 179.4 122.7 23.9 20 B LEU CB 650 180.2 121.5 23.5 20 B LEU CG 650 179.5 120.5 22.6 18 B LEU CD1 650 180.5 119.5 22.1 18 B LEU CD2 650 178.4 119.7 23.4 17 B LEU C 650 179.6 123.2 25.3 20 B LEU O 650 179.0 122.7 26.2 21 B ALA N 651 180.6 124.1 25.6 21 B ALA CA 651 180.9 124.5 27.0 20 B ALA CB 651 182.1 125.3 27.1 19 B ALA C 651 179.7 125.2 27.6 20 B ALA O 651 179.3 125.0 28.7 20 B PRO N 652 179.1 126.2 26.9 20 B PRO CD 652 179.8 127.0 25.7 20 B PRO CA 652 178.0 127.0 27.4 21 B PRO CB 652 177.8 128.0 26.3 21 B PRO CG 652 179.1 128.3 25.9 20 B PRO C 652 176.8 126.0 27.4 22 B PRO O 652 176.0 126.0 28.4 23 B THR N 653 176.6 125.1 26.4 21 B THR CA 653 175.6 124.1 26.4 20 B THR CB 653 175.7 123.2 25.2 20 B THR OG1 653 175.7 124.0 24.0 21 B THR CG2 653 174.6 122.2 25.2 19 B THR C 653 175.6 123.2 27.7 21 B THR O 653 174.6 123.0 28.3 22 B TYR N 654 176.8 122.8 28.1 20 B TYR CA 654 176.9 121.9 29.2 20 B TYR CB 654 178.4 121.5 29.5 19 B TYR CG 654 178.7 121.0 30.8 18 B TYR CD1 654 178.4 119.7 31.2 18 B TYR CE1 654 178.8 119.3 32.5 19 B TYR CD2 654 179.3 121.9 31.8 18 B TYR CE2 654 179.6 121.4 33.0 19 B TYR CZ 654 179.4 120.1 33.4 19 B TYR OH 654 179.8 119.6 34.6 19 B TYR C 654 176.4 122.8 30.4 21 B TYR O 654 175.6 122.3 31.1 22 B ALA N 655 176.9 124.0 30.5 23 B ALA CA 655 176.6 124.9 31.6 23 B ALA CB 655 177.5 126.1 31.5 22 B ALA C 655 175.1 125.3 31.7 23 B ALA O 655 174.6 125.3 32.8 23 B ALA N 656 174.5 125.5 30.5 22 B ALA CA 656 173.1 125.9 30.5 23 B ALA CB 656 172.7 126.2 29.1 21 B ALA C 656 172.3 124.7 31.1 24 B ALA O 656 171.7 124.8 32.1 24 B VAL N 657 172.4 123.6 30.3 26 B VAL CA 657 171.7 122.4 30.7 27 B VAL CB 657 172.1 121.2 29.8 26 B VAL CG1 657 171.3 119.9 30.2 27 B VAL CG2 657 171.8 121.6 28.4 26 B VAL C 657 171.9 122.1 32.2 27 B VAL O 657 171.0 121.7 32.9 28 B ASN N 658 173.1 122.2 32.8 27 B ASN CA 658 173.4 122.0 34.2 28 B ASN CB 658 174.8 122.0 34.5 27 B ASN CG 658 175.5 120.7 34.6 27 B ASN OD1 658 175.1 119.8 33.9 26 B ASN ND2 658 176.4 120.6 35.6 28 B ASN C 658 172.6 122.9 35.0 29 B ASN O 658 172.0 122.6 36.0 30 B ALA N 659 172.6 124.2 34.6 29 B ALA CA 659 171.9 125.3 35.3 28 B ALA CB 659 172.1 126.6 34.7 28 B ALA C 659 170.4 124.9 35.4 28 B ALA O 659 169.9 124.6 36.4 28 B LEU N 660 169.9 124.8 34.2 28 B LEU CA 660 168.5 124.4 34.0 28 B LEU CB 660 168.2 124.2 32.5 27 B LEU CG 660 168.2 125.4 31.7 26 B LEU CD1 660 167.8 125.2 30.3 26 B LEU CD2 660 167.3 126.5 32.3 26 B LEU C 660 168.1 123.2 34.9 30 B LEU O 660 167.0 123.2 35.5 31 B CYS N 661 169.0 122.2 35.0 32 B CYS CA 661 168.7 121.1 35.8 33 B CYS CB 661 169.6 119.9 35.4 32 B CYS SG 661 169.1 119.2 33.9 31 B CYS C 661 168.8 121.4 37.3 35 B CYS O 661 168.0 120.8 38.1 36 B ILE N 662 169.6 122.3 37.7 37 B ILE CA 662 169.7 122.7 39.1 39 B ILE CB 662 170.9 123.6 39.4 39 B ILE CG2 662 171.0 123.9 40.9 39 B ILE CG1 662 172.2 123.0 38.9 39 B ILE CD1 662 173.5 123.7 39.3 39 B ILE C 662 168.4 123.4 39.5 39 B ILE O 662 167.9 123.2 40.6 40 B ILE N 663 167.8 124.2 38.6 39 B ILE CA 663 166.5 124.8 38.8 39 B ILE CB 663 166.3 125.9 37.7 38 B ILE CG2 663 164.9 126.4 37.8 38 B ILE CG1 663 167.3 127.0 37.8 37 B ILE CD1 663 167.1 128.0 36.7 37 B ILE C 663 165.4 123.8 38.9 39 B ILE O 663 164.4 124.0 39.4 40 B GLY N 664 165.7 122.6 38.3 39 B GLY CA 664 164.8 121.5 38.2 40 B GLY C 664 163.3 121.7 38.1 39 B GLY O 664 162.5 120.9 38.6 40 B THR N 665 162.8 122.8 37.5 39 B THR CA 665 161.4 123.0 37.4 40 B THR CB 665 161.0 124.5 37.6 39 B THR OG1 665 161.2 125.2 36.3 38 B THR CG2 665 161.8 125.1 38.7 39 B THR C 665 161.0 122.6 36.0 41 B THR O 665 161.8 122.5 35.1 41 B GLU N 666 159.7 122.3 35.9 44 B GLU CA 666 159.1 122.0 34.6 46 B GLU CB 666 157.7 121.4 34.7 48 B GLU CG 666 157.6 119.9 34.8 50 B GLU CD 666 158.2 119.2 36.1 50 B GLU OE1 666 158.3 119.9 37.2 51 B GLU OE2 666 158.6 118.0 36.1 51 B GLU C 666 159.2 123.1 33.6 47 B GLU O 666 158.9 123.0 32.4 47 B GLU N 667 159.7 124.3 34.2 46 B GLU CA 667 159.9 125.5 33.3 46 B GLU CB 667 159.8 126.7 34.2 47 B GLU CG 667 160.2 128.0 33.4 47 B GLU CD 667 160.1 129.3 34.2 48 B GLU OE1 667 160.2 129.2 35.4 48 B GLU OE2 667 159.8 130.3 33.5 49 B GLU C 667 161.3 125.4 32.8 44 B GLU O 667 161.5 125.6 31.6 45 B ALA N 668 162.2 125.1 33.7 43 B ALA CA 668 163.6 125.0 33.3 40 B ALA CB 668 164.5 124.6 34.5 41 B ALA C 668 163.7 123.9 32.3 39 B ALA O 668 164.1 124.1 31.1 39 B TYR N 669 163.3 122.6 32.6 38 B TYR CA 669 163.4 121.5 31.7 37 B TYR CB 669 162.7 120.3 32.3 35 B TYR CG 669 163.2 119.7 33.6 32 B TYR CD1 669 162.3 119.2 34.6 31 B TYR CE1 669 162.7 118.8 35.8 30 B TYR CD2 669 164.6 119.8 34.0 31 B TYR CE2 669 165.0 119.3 35.3 30 B TYR CZ 669 164.1 118.8 36.2 29 B TYR OH 669 164.4 118.4 37.4 27 B TYR C 669 162.8 121.8 30.4 37 B TYR O 669 163.4 121.5 29.3 38 B ASN N 670 161.8 122.6 30.4 38 B ASN CA 670 161.1 122.9 29.1 39 B ASN CB 670 159.7 123.4 29.4 42 B ASN CG 670 158.7 122.3 29.5 44 B ASN OD1 670 159.1 121.2 30.1 45 B ASN ND2 670 157.5 122.5 28.9 45 B ASN C 670 161.9 123.9 28.2 39 B ASN O 670 161.5 124.1 27.1 39 B VAL N 671 162.9 124.6 28.8 38 B VAL CA 671 163.7 125.5 28.0 37 B VAL CB 671 164.7 126.2 28.9 38 B VAL CG1 671 165.6 127.0 28.0 38 B VAL CG2 671 164.1 127.0 30.0 38 B VAL C 671 164.4 124.7 26.9 36 B VAL O 671 164.3 125.1 25.7 36 B ILE N 672 165.1 123.6 27.3 35 B ILE CA 672 165.9 122.8 26.4 33 B ILE CB 672 166.5 121.6 27.2 31 B ILE CG2 672 167.5 120.9 26.3 32 B ILE CG1 672 167.2 122.2 28.4 31 B ILE CD1 672 167.8 121.1 29.3 30 B ILE C 672 165.1 122.1 25.3 33 B ILE O 672 164.1 121.4 25.5 35 B ASN N 673 165.5 122.4 24.0 34 B ASN CA 673 164.9 121.9 22.8 35 B ASN CB 673 165.0 122.9 21.7 35 B ASN CG 673 164.5 122.3 20.4 35 B ASN OD1 673 164.7 121.2 20.0 36 B ASN ND2 673 163.9 123.2 19.6 34 B ASN C 673 165.6 120.6 22.5 37 B ASN O 673 166.6 120.6 21.7 38 B ARG N 674 165.2 119.5 23.1 38 B ARG CA 674 165.8 118.2 22.9 38 B ARG CB 674 165.1 117.1 23.8 37 B ARG CG 674 165.1 117.4 25.2 38 B ARG CD 674 164.2 116.4 26.0 39 B ARG NE 674 164.5 115.0 25.8 39 B ARG CZ 674 163.9 114.2 24.9 39 B ARG NH1 674 162.9 114.6 24.1 39 B ARG NH2 674 164.4 113.0 24.8 38 B ARG C 674 166.0 117.6 21.5 40 B ARG O 674 167.0 117.0 21.3 40 B GLU N 675 165.1 117.9 20.6 41 B GLU CA 675 165.3 117.3 19.3 44 B GLU CB 675 164.0 117.4 18.5 47 B GLU CG 675 163.0 118.6 18.9 51 B GLU CD 675 162.3 118.4 20.3 53 B GLU OE1 675 162.6 119.2 21.2 54 B GLU OE2 675 161.5 117.4 20.4 55 B GLU C 675 166.4 118.0 18.6 43 B GLU O 675 167.1 117.4 17.8 42 B LYS N 676 166.6 119.3 18.9 42 B LYS CA 676 167.6 120.1 18.2 41 B LYS CB 676 167.2 121.5 18.0 42 B LYS CG 676 166.6 121.7 16.6 43 B LYS CD 676 166.6 123.1 16.1 46 B LYS CE 676 165.7 124.0 17.0 48 B LYS NZ 676 165.5 125.4 16.6 49 B LYS C 676 168.9 120.0 19.0 39 B LYS O 676 170.0 120.1 18.3 39 B LEU N 677 168.9 119.8 20.3 36 B LEU CA 677 170.1 119.7 21.0 35 B LEU CB 677 169.8 119.4 22.5 33 B LEU CG 677 170.9 119.0 23.4 32 B LEU CD1 677 172.2 119.8 23.2 33 B LEU CD2 677 170.5 119.1 24.8 32 B LEU C 677 170.9 118.5 20.4 35 B LEU O 677 172.1 118.6 20.2 35 B LEU N 678 170.2 117.5 20.1 36 B LEU CA 678 170.8 116.2 19.5 36 B LEU CB 678 169.7 115.1 19.6 36 B LEU CG 678 169.8 113.7 19.0 36 B LEU CD1 678 169.2 113.6 17.6 36 B LEU CD2 678 171.2 113.1 19.0 36 B LEU C 678 171.2 116.5 18.1 35 B LEU O 678 172.3 116.0 17.7 35 B GLN N 679 170.4 117.2 17.3 36 B GLN CA 679 170.7 117.6 16.0 37 B GLN CB 679 169.7 118.6 15.4 39 B GLN CG 679 169.8 119.0 14.0 41 B GLN CD 679 168.6 119.7 13.5 43 B GLN OE1 679 168.7 120.9 13.0 44 B GLN NE2 679 167.4 119.2 13.7 43 B GLN C 679 172.1 118.2 15.9 36 B GLN O 679 172.9 117.9 15.0 37 B TYR N 680 172.4 119.0 16.9 33 B TYR CA 680 173.6 119.7 17.1 30 B TYR CB 680 173.5 120.7 18.3 29 B TYR CG 680 174.7 121.5 18.6 26 B TYR CD1 680 175.3 122.4 17.7 25 B TYR CE1 680 176.4 123.2 18.0 24 B TYR CD2 680 175.2 121.6 19.9 25 B TYR CE2 680 176.2 122.3 20.3 24 B TYR CZ 680 176.8 123.1 19.3 24 B TYR OH 680 177.9 124.0 19.7 24 B TYR C 680 174.7 118.7 17.5 28 B TYR O 680 175.7 118.7 16.8 26 B LEU N 681 174.5 117.9 18.6 27 B LEU CA 681 175.6 117.0 19.0 27 B LEU CB 681 175.1 116.1 20.1 25 B LEU CG 681 174.7 116.8 21.4 25 B LEU CD1 681 174.2 115.8 22.5 23 B LEU CD2 681 175.9 117.5 21.9 24 B LEU C 681 176.1 116.2 17.8 28 B LEU O 681 177.2 115.8 17.6 28 B TYR N 682 175.1 115.9 16.8 29 B TYR CA 682 175.5 115.2 15.6 30 B TYR CB 682 174.3 114.7 14.8 32 B TYR CG 682 173.8 113.3 15.2 33 B TYR CD1 682 172.5 113.1 15.6 34 B TYR CE1 682 172.0 111.9 15.9 34 B TYR CD2 682 174.6 112.2 15.1 34 B TYR CE2 682 174.2 110.9 15.5 34 B TYR CZ 682 172.9 110.8 15.9 34 B TYR OH 682 172.4 109.5 16.2 33 B TYR C 682 176.4 116.1 14.8 29 B TYR O 682 177.3 115.6 14.1 30 B SER N 683 176.2 117.4 14.8 29 B SER CA 683 176.9 118.3 14.0 28 B SER CB 683 176.2 119.7 13.9 27 B SER OG 683 176.2 120.4 15.1 26 B SER C 683 178.4 118.5 14.4 27 B SER O 683 179.2 119.1 13.7 27 B LEU N 684 178.7 118.0 15.6 26 B LEU CA 684 180.1 118.1 16.1 26 B LEU CB 684 180.0 118.7 17.5 24 B LEU CG 684 179.1 120.0 17.7 22 B LEU CD1 684 179.1 120.4 19.1 21 B LEU CD2 684 179.6 121.1 16.8 20 B LEU C 684 180.8 116.7 16.1 27 B LEU O 684 182.0 116.7 16.0 28 B LYS N 685 180.0 115.7 16.1 27 B LYS CA 685 180.5 114.3 16.1 26 B LYS CB 685 179.4 113.3 15.9 26 B LYS CG 685 179.5 112.0 16.7 25 B LYS CD 685 180.9 111.5 16.7 26 B LYS CE 685 181.1 110.3 17.6 27 B LYS NZ 685 180.3 109.1 17.1 28 B LYS C 685 181.5 114.2 14.9 25 B LYS O 685 181.3 114.7 13.8 25 B GLN N 686 182.6 113.5 15.2 25 B GLN CA 686 183.7 113.3 14.2 26 B GLN CB 686 185.0 113.9 14.8 25 B GLN CG 686 185.0 115.4 15.0 26 B GLN CD 686 184.8 116.1 13.7 27 B GLN OE1 686 185.8 116.3 13.0 28 B GLN NE2 686 183.6 116.7 13.5 27 B GLN C 686 183.8 111.8 14.0 27 B GLN O 686 183.4 111.0 14.8 28 B PRO N 687 184.5 111.5 12.8 26 B PRO CD 687 184.9 112.3 11.7 27 B PRO CA 687 184.6 110.1 12.5 26 B PRO CB 687 185.4 110.1 11.2 26 B PRO CG 687 184.8 111.3 10.6 27 B PRO C 687 185.5 109.4 13.6 26 B PRO O 687 185.1 108.3 14.0 27 B ASP N 688 186.5 110.0 14.1 25 B ASP CA 688 187.3 109.3 15.1 25 B ASP CB 688 188.7 109.9 15.2 26 B ASP CG 688 188.8 111.3 15.7 27 B ASP OD1 688 187.8 112.0 15.8 28 B ASP OD2 688 189.9 111.7 16.0 28 B ASP C 688 186.6 109.3 16.4 24 B ASP O 688 187.3 109.0 17.4 25 B GLY N 689 185.4 109.6 16.5 22 B GLY CA 689 184.6 109.6 17.7 21 B GLY C 689 184.7 110.8 18.6 20 B GLY O 689 184.1 110.9 19.6 21 B SER N 690 185.4 111.8 18.1 20 B SER CA 690 185.6 113.0 18.9 19 B SER CB 690 186.9 113.7 18.7 18 B SER OG 690 187.2 114.0 17.4 17 B SER C 690 184.4 114.0 18.5 19 B SER O 690 183.7 113.7 17.6 20 B PHE N 691 184.3 115.1 19.2 19 B PHE CA 691 183.3 116.1 19.0 19 B PHE CB 691 182.3 116.2 20.1 20 B PHE CG 691 181.4 115.0 20.2 19 B PHE CD1 691 181.7 113.9 21.0 19 B PHE CD2 691 180.1 115.1 19.6 19 B PHE CE1 691 180.8 112.9 21.1 19 B PHE CE2 691 179.2 114.0 19.7 19 B PHE CZ 691 179.6 112.9 20.5 19 B PHE C 691 184.0 117.5 18.9 18 B PHE O 691 185.0 117.8 19.6 18 B LEU N 692 183.6 118.3 17.9 18 B LEU CA 692 184.2 119.7 17.9 18 B LEU CB 692 183.6 120.4 16.7 17 B LEU CG 692 183.8 119.8 15.3 16 B LEU CD1 692 183.1 120.7 14.3 15 B LEU CD2 692 185.3 119.9 15.0 16 B LEU C 692 183.6 120.3 19.1 21 B LEU O 692 182.6 119.8 19.7 22 B MET N 693 184.1 121.5 19.6 21 B MET CA 693 183.6 122.2 20.7 20 B MET CB 693 184.6 123.1 21.4 19 B MET CG 693 185.6 122.3 22.3 20 B MET SD 693 184.7 121.5 23.6 21 B MET CE 693 184.3 122.8 24.8 20 B MET C 693 182.4 123.0 20.2 20 B MET O 693 181.5 123.4 20.9 21 B HIS N 694 182.5 123.4 18.9 21 B HIS CA 694 181.4 124.1 18.2 21 B HIS CB 694 181.4 125.5 18.7 22 B HIS CG 694 182.6 126.3 18.4 23 B HIS CD2 694 183.8 126.4 19.1 23 B HIS ND1 694 182.7 127.3 17.4 23 B HIS CE1 694 183.9 127.8 17.4 24 B HIS NE2 694 184.6 127.3 18.4 24 B HIS C 694 181.8 124.1 16.7 21 B HIS O 694 182.9 123.7 16.3 22 B VAL N 695 180.9 124.4 15.8 21 B VAL CA 695 181.2 124.3 14.4 21 B VAL CB 695 180.0 124.8 13.5 22 B VAL CG1 695 180.4 124.8 12.1 23 B VAL CG2 695 178.8 123.9 13.7 21 B VAL C 695 182.4 125.2 14.0 21 B VAL O 695 182.5 126.3 14.5 23 B GLY N 696 183.3 124.6 13.3 21 B GLY CA 696 184.5 125.4 12.9 21 B GLY C 696 185.5 125.5 14.1 21 B GLY O 696 186.6 125.9 13.9 22 B GLY N 697 185.1 125.0 15.3 21 B GLY CA 697 185.9 125.1 16.5 20 B GLY C 697 186.9 123.9 16.7 20 B GLY O 697 187.1 123.0 15.9 20 B GLU N 698 187.6 124.0 17.8 20 B GLU CA 698 188.6 123.0 18.3 21 B GLU CB 698 189.6 123.7 19.3 22 B GLU CG 698 189.0 123.9 20.7 23 B GLU CD 698 188.1 125.0 21.0 24 B GLU OE1 698 187.7 125.8 20.0 24 B GLU OE2 698 187.7 125.3 22.2 25 B GLU C 698 188.0 121.7 18.8 21 B GLU O 698 186.8 121.6 19.1 21 B VAL N 699 188.9 120.7 19.0 20 B VAL CA 699 188.5 119.4 19.5 19 B VAL CB 699 188.6 118.3 18.4 19 B VAL CG1 699 188.8 116.9 18.9 18 B VAL CG2 699 187.4 118.3 17.5 19 B VAL C 699 189.4 118.9 20.7 20 B VAL O 699 190.6 119.0 20.6 19 B ASP N 700 188.7 118.3 21.7 20 B ASP CA 700 189.4 117.8 22.9 20 B ASP CB 700 190.4 118.8 23.5 21 B ASP CG 700 189.7 119.9 24.2 22 B ASP OD1 700 188.8 119.7 25.1 22 B ASP OD2 700 190.0 121.1 23.9 23 B ASP C 700 188.4 117.2 23.9 21 B ASP O 700 187.2 117.5 23.8 21 B VAL N 701 188.9 116.4 24.8 20 B VAL CA 701 188.0 115.8 25.8 21 B VAL CB 701 188.7 115.0 27.0 20 B VAL CG1 701 188.7 113.6 26.7 20 B VAL CG2 701 190.0 115.6 27.2 21 B VAL C 701 186.9 116.6 26.4 22 B VAL O 701 185.8 116.0 26.7 23 B ARG N 702 187.1 117.9 26.6 23 B ARG CA 702 186.0 118.7 27.2 23 B ARG CB 702 186.3 120.2 27.1 23 B ARG CG 702 187.4 120.7 28.1 23 B ARG CD 702 187.8 122.1 27.7 24 B ARG NE 702 188.2 122.2 26.2 25 B ARG CZ 702 187.9 123.2 25.4 25 B ARG NH1 702 188.2 123.1 24.1 25 B ARG NH2 702 187.3 124.3 25.9 26 B ARG C 702 184.7 118.4 26.4 24 B ARG O 702 183.6 118.1 27.0 24 B SER N 703 184.8 118.3 25.1 23 B SER CA 703 183.6 118.0 24.2 24 B SER CB 703 183.9 118.3 22.7 24 B SER OG 703 184.7 117.2 22.2 25 B SER C 703 182.9 116.7 24.4 24 B SER O 703 181.7 116.6 24.3 26 B ALA N 704 183.7 115.6 24.6 24 B ALA CA 704 183.2 114.3 24.8 23 B ALA CB 704 184.3 113.3 24.9 23 B ALA C 704 182.3 114.3 26.1 23 B ALA O 704 181.3 113.6 26.2 22 B TYR N 705 182.8 115.0 27.1 23 B TYR CA 705 182.2 115.2 28.4 24 B TYR CB 705 183.1 115.6 29.4 24 B TYR CG 705 182.5 116.0 30.7 23 B TYR CD1 705 181.8 115.0 31.5 23 B TYR CE1 705 181.3 115.4 32.8 23 B TYR CD2 705 182.5 117.3 31.2 23 B TYR CE2 705 182.0 117.6 32.4 23 B TYR CZ 705 181.4 116.7 33.2 23 B TYR OH 705 180.9 117.0 34.4 22 B TYR C 705 180.9 116.1 28.3 24 B TYR O 705 179.9 115.9 29.0 24 B CYS N 706 181.1 117.2 27.6 24 B CYS CA 706 179.9 118.1 27.6 24 B CYS CB 706 180.3 119.4 26.8 25 B CYS SG 706 181.5 120.4 27.6 25 B CYS C 706 178.8 117.4 26.9 25 B CYS O 706 177.7 117.3 27.5 26 B ALA N 707 179.1 116.8 25.7 24 B ALA CA 707 178.1 116.0 25.0 23 B ALA CB 707 178.7 115.5 23.7 21 B ALA C 707 177.5 114.8 25.8 22 B ALA O 707 176.3 114.7 26.0 21 B ALA N 708 178.4 114.0 26.4 23 B ALA CA 708 177.9 112.9 27.2 24 B ALA CB 708 179.1 112.0 27.7 24 B ALA C 708 177.0 113.3 28.4 26 B ALA O 708 176.1 112.5 28.8 27 B SER N 709 177.3 114.5 29.0 26 B SER CA 709 176.5 115.0 30.1 25 B SER CB 709 177.3 116.1 30.8 25 B SER OG 709 176.6 116.5 32.0 24 B SER C 709 175.1 115.5 29.7 26 B SER O 709 174.1 115.1 30.3 26 B VAL N 710 175.1 116.3 28.7 27 B VAL CA 710 173.8 116.9 28.2 27 B VAL CB 710 174.0 118.1 27.3 26 B VAL CG1 710 174.9 119.2 27.9 25 B VAL CG2 710 174.6 117.7 26.0 26 B VAL C 710 172.9 115.9 27.5 27 B VAL O 710 171.7 115.8 27.8 27 B ALA N 711 173.5 115.1 26.6 28 B ALA CA 711 172.7 114.0 25.9 28 B ALA CB 711 173.5 113.3 24.9 28 B ALA C 711 172.1 113.0 26.9 29 B ALA O 711 171.0 112.6 26.7 29 B SER N 712 172.9 112.7 27.9 30 B SER CA 712 172.4 111.7 28.9 31 B SER CB 712 173.5 111.1 29.8 30 B SER OG 712 174.2 112.0 30.7 30 B SER C 712 171.3 112.3 29.8 31 B SER O 712 170.2 111.7 29.9 32 B LEU N 713 171.6 113.5 30.4 31 B LEU CA 713 170.6 114.1 31.2 32 B LEU CB 713 171.1 115.5 31.8 31 B LEU CG 713 172.1 115.4 32.9 30 B LEU CD1 713 172.4 116.8 33.4 29 B LEU CD2 713 171.5 114.7 34.1 30 B LEU C 713 169.3 114.3 30.5 33 B LEU O 713 168.2 114.0 31.1 34 B THR N 714 169.3 114.8 29.3 34 B THR CA 714 168.1 115.0 28.5 33 B THR CB 714 168.2 116.3 27.6 33 B THR OG1 714 169.4 116.1 26.8 33 B THR CG2 714 168.4 117.5 28.4 32 B THR C 714 167.6 113.8 27.8 34 B THR O 714 166.7 113.9 27.0 35 B ASN N 715 168.2 112.6 28.0 34 B ASN CA 715 167.8 111.4 27.4 33 B ASN CB 715 166.5 110.9 28.0 34 B ASN CG 715 165.8 109.7 27.4 35 B ASN OD1 715 166.5 108.8 26.9 37 B ASN ND2 715 164.5 109.6 27.4 36 B ASN C 715 167.7 111.5 25.9 32 B ASN O 715 166.6 111.4 25.3 32 B ILE N 716 168.8 111.8 25.2 31 B ILE CA 716 168.7 111.9 23.7 31 B ILE CB 716 169.0 113.4 23.3 31 B ILE CG2 716 167.8 114.2 23.6 31 B ILE CG1 716 170.2 113.9 23.9 31 B ILE CD1 716 170.7 115.2 23.2 31 B ILE C 716 169.8 111.1 23.1 30 B ILE O 716 170.2 111.3 22.0 30 B ILE N 717 170.4 110.2 23.9 30 B ILE CA 717 171.5 109.4 23.5 31 B ILE CB 717 172.2 108.6 24.6 31 B ILE CG2 717 173.3 107.7 24.1 31 B ILE CG1 717 172.7 109.6 25.6 31 B ILE CD1 717 173.6 109.0 26.7 30 B ILE C 717 170.9 108.3 22.5 33 B ILE O 717 170.1 107.5 22.9 33 B THR N 718 171.2 108.5 21.2 33 B THR CA 718 170.7 107.6 20.2 34 B THR CB 718 170.8 108.2 18.8 33 B THR OG1 718 172.2 108.5 18.5 33 B THR CG2 718 170.0 109.5 18.8 32 B THR C 718 171.7 106.4 20.3 36 B THR O 718 172.3 106.2 21.3 37 B PRO N 719 171.8 105.5 19.3 38 B PRO CD 719 170.7 105.2 18.3 39 B PRO CA 719 172.7 104.4 19.4 38 B PRO CB 719 172.0 103.4 18.5 39 B PRO CG 719 170.6 103.8 18.5 39 B PRO C 719 174.1 104.7 18.8 38 B PRO O 719 175.1 104.3 19.4 39 B ASP N 720 174.1 105.4 17.7 39 B ASP CA 720 175.4 105.8 17.1 39 B ASP CB 720 175.3 105.7 15.6 41 B ASP CG 720 174.3 106.8 15.1 41 B ASP OD1 720 174.4 107.2 13.9 42 B ASP OD2 720 173.4 107.2 15.9 42 B ASP C 720 176.0 107.1 17.5 39 B ASP O 720 177.0 107.5 17.0 39 B LEU N 721 175.3 107.9 18.4 38 B LEU CA 721 175.8 109.2 18.8 38 B LEU CB 721 174.8 109.8 19.9 36 B LEU CG 721 175.2 111.2 20.3 36 B LEU CD1 721 175.3 112.1 19.1 35 B LEU CD2 721 174.1 111.7 21.3 35 B LEU C 721 177.2 109.1 19.3 38 B LEU O 721 178.1 109.8 18.8 38 B PHE N 722 177.4 108.3 20.4 38 B PHE CA 722 178.8 108.2 20.9 38 B PHE CB 722 178.6 108.1 22.5 39 B PHE CG 722 178.1 109.4 23.1 40 B PHE CD1 722 176.7 109.4 23.4 40 B PHE CD2 722 178.9 110.5 23.2 41 B PHE CE1 722 176.2 110.6 23.9 40 B PHE CE2 722 178.3 111.7 23.7 41 B PHE CZ 722 177.0 111.7 24.0 41 B PHE C 722 179.6 107.1 20.4 39 B PHE O 722 180.5 106.6 21.0 40 B GLU N 723 179.3 106.7 19.2 39 B GLU CA 723 180.0 105.6 18.5 39 B GLU CB 723 179.4 105.3 17.2 42 B GLU CG 723 179.5 103.8 16.8 45 B GLU CD 723 179.2 103.0 18.1 47 B GLU OE1 723 178.1 103.1 18.6 48 B GLU OE2 723 180.2 102.3 18.6 48 B GLU C 723 181.5 105.9 18.4 36 B GLU O 723 181.9 106.9 17.7 35 B GLY N 724 182.3 105.2 19.1 34 B GLY CA 724 183.7 105.4 19.0 32 B GLY C 724 184.3 106.4 20.0 30 B GLY O 724 185.5 106.5 20.0 30 B THR N 725 183.5 107.1 20.7 28 B THR CA 725 184.1 108.2 21.6 27 B THR CB 725 183.1 109.4 21.8 27 B THR OG1 725 182.7 109.5 23.2 28 B THR CG2 725 181.9 109.3 20.9 27 B THR C 725 184.7 107.6 22.9 26 B THR O 725 185.5 108.3 23.5 26 B ALA N 726 184.4 106.4 23.2 25 B ALA CA 726 185.0 105.9 24.4 25 B ALA CB 726 184.3 104.6 24.9 26 B ALA C 726 186.4 105.5 24.0 25 B ALA O 726 187.4 105.6 24.8 25 B GLU N 727 186.5 105.0 22.7 25 B GLU CA 727 187.8 104.6 22.2 24 B GLU CB 727 187.6 104.0 20.8 25 B GLU CG 727 187.2 102.5 20.7 26 B GLU CD 727 185.7 102.3 21.2 26 B GLU OE1 727 185.6 101.2 21.9 27 B GLU OE2 727 184.8 103.0 20.9 26 B GLU C 727 188.7 105.8 22.1 23 B GLU O 727 189.8 105.9 22.6 24 B TRP N 728 188.2 106.9 21.4 22 B TRP CA 728 189.0 108.1 21.3 21 B TRP CB 728 188.2 109.2 20.6 20 B TRP CG 728 189.0 110.3 20.2 20 B TRP CD2 728 189.3 111.5 21.0 20 B TRP CE2 728 190.1 112.3 20.2 21 B TRP CE3 728 188.8 112.0 22.2 20 B TRP CD1 728 189.8 110.5 19.1 19 B TRP NE1 728 190.4 111.7 19.1 20 B TRP CZ2 728 190.6 113.6 20.7 21 B TRP CZ3 728 189.2 113.2 22.7 21 B TRP CH2 728 190.1 114.0 21.9 20 B TRP C 728 189.4 108.6 22.7 21 B TRP O 728 190.6 108.8 22.9 21 B ILE N 729 188.4 108.8 23.6 20 B ILE CA 729 188.8 109.2 25.0 19 B ILE CB 729 187.6 109.3 25.9 17 B ILE CG2 729 188.1 109.7 27.3 15 B ILE CG1 729 186.6 110.3 25.4 17 B ILE CD1 729 185.3 110.3 26.2 18 B ILE C 729 189.9 108.3 25.6 20 B ILE O 729 190.8 108.8 26.3 21 B ALA N 730 189.9 107.1 25.3 22 B ALA CA 730 190.9 106.1 25.8 23 B ALA CB 730 190.4 104.7 25.5 24 B ALA C 730 192.3 106.4 25.2 24 B ALA O 730 193.3 106.1 25.8 25 B ARG N 731 192.3 107.0 24.0 23 B ARG CA 731 193.6 107.4 23.4 23 B ARG CB 731 193.4 107.5 21.9 23 B ARG CG 731 193.1 106.3 21.2 23 B ARG CD 731 193.5 106.3 19.8 22 B ARG NE 731 192.7 107.3 19.0 23 B ARG CZ 731 193.2 108.2 18.2 24 B ARG NH1 731 194.5 108.4 18.2 24 B ARG NH2 731 192.4 109.0 17.5 24 B ARG C 731 194.2 108.6 24.0 24 B ARG O 731 195.3 109.0 23.6 24 B CYS N 732 193.5 109.2 24.9 22 B CYS CA 732 194.0 110.4 25.6 21 B CYS CB 732 192.8 111.4 25.9 20 B CYS SG 732 192.1 111.9 24.3 22 B CYS C 732 194.7 110.0 26.8 21 B CYS O 732 195.5 110.9 27.4 23 B GLN N 733 194.6 108.8 27.3 20 B GLN CA 733 195.4 108.4 28.5 19 B GLN CB 733 194.8 107.1 29.1 19 B GLN CG 733 195.4 106.6 30.4 18 B GLN CD 733 194.7 105.4 31.0 19 B GLN OE1 733 194.1 104.6 30.2 19 B GLN NE2 733 194.8 105.2 32.3 18 B GLN C 733 196.8 108.2 28.0 20 B GLN O 733 197.0 107.5 27.1 21 B ASN N 734 197.8 108.8 28.7 19 B ASN CA 734 199.2 108.7 28.3 18 B ASN CB 734 199.8 110.1 28.0 17 B ASN CG 734 200.2 110.8 29.3 17 B ASN OD1 734 199.9 110.4 30.4 16 B ASN ND2 734 200.9 111.9 29.1 17 B ASN C 734 200.1 107.9 29.3 17 B ASN O 734 199.6 107.3 30.2 17 B TRP N 735 201.4 107.9 29.0 17 B TRP CA 735 202.3 107.2 29.9 18 B TRP CB 735 203.7 107.4 29.4 17 B TRP CG 735 204.0 108.9 29.3 18 B TRP CD2 735 204.8 109.7 30.3 18 B TRP CE2 735 204.8 111.0 29.8 18 B TRP CE3 735 205.4 109.4 31.5 18 B TRP CD1 735 203.7 109.7 28.3 19 B TRP NE1 735 204.1 111.0 28.6 19 B TRP CZ2 735 205.4 112.0 30.4 19 B TRP CZ3 735 206.0 110.4 32.2 18 B TRP CH2 735 206.0 111.7 31.6 18 B TRP C 735 202.2 107.5 31.4 19 B TRP O 735 202.7 106.8 32.3 21 B GLU N 736 201.7 108.7 31.7 19 B GLU CA 736 201.6 109.2 33.1 19 B GLU CB 736 201.4 110.7 33.2 19 B GLU CG 736 202.6 111.5 32.8 20 B GLU CD 736 202.2 113.0 32.6 20 B GLU OE1 736 201.9 113.3 31.4 19 B GLU OE2 736 202.2 113.8 33.5 20 B GLU C 736 200.4 108.5 33.9 18 B GLU O 736 200.5 108.5 35.1 20 B GLY N 737 199.4 108.0 33.1 16 B GLY CA 737 198.3 107.4 33.8 14 B GLY C 737 197.1 108.4 33.7 13 B GLY O 737 196.0 108.0 33.6 14 B GLY N 738 197.4 109.7 33.6 12 B GLY CA 738 196.4 110.7 33.4 11 B GLY C 738 195.9 110.7 31.9 11 B GLY O 738 196.3 110.0 31.1 10 B ILE N 739 195.0 111.7 31.7 10 B ILE CA 739 194.4 111.9 30.4  9 B ILE CB 739 192.9 111.7 30.4  9 B ILE CG2 739 192.3 112.1 29.1  9 B ILE CG1 739 192.6 110.2 30.8  8 B ILE CD1 739 191.1 109.8 30.8  7 B ILE C 739 194.8 113.3 29.9  9 B ILE O 739 194.8 114.2 30.7 10 B GLY N 740 195.0 113.5 28.6  9 B GLY CA 740 195.3 114.8 28.0  9 B GLY C 740 194.2 115.3 27.2 11 B GLY O 740 193.1 114.7 27.0 11 B GLY N 741 194.3 116.5 26.7 12 B GLY CA 741 193.3 117.1 25.9 14 B GLY C 741 193.0 116.4 24.6 16 B GLY O 741 191.8 116.3 24.2 16 B VAL N 742 194.0 115.9 24.0 17 B VAL CA 742 194.0 115.1 22.7 16 B VAL CB 742 194.3 116.0 21.5 16 B VAL CG1 742 193.2 117.0 21.3 15 B VAL CG2 742 195.6 116.7 21.6 16 B VAL C 742 195.1 114.1 22.9 18 B VAL O 742 196.1 114.4 23.7 18 B PRO N 743 195.1 113.0 22.2 17 B PRO CD 743 194.1 112.5 21.2 17 B PRO CA 743 196.2 112.0 22.3 17 B PRO CB 743 195.8 111.0 21.2 17 B PRO CG 743 194.4 111.0 21.1 16 B PRO C 743 197.6 112.5 22.1 17 B PRO O 743 197.9 113.3 21.2 18 B GLY N 744 198.5 112.2 23.0 17 B GLY CA 744 199.9 112.7 22.9 17 B GLY C 744 200.2 113.7 23.9 19 B GLY O 744 201.4 113.8 24.3 18 B MET N 745 199.2 114.5 24.3 20 B MET CA 745 199.4 115.6 25.3 20 B MET CB 745 198.2 116.5 25.3 20 B MET CG 745 198.3 117.7 24.3 21 B MET SD 745 200.0 118.3 24.1 23 B MET CE 745 200.2 119.1 25.6 23 B MET C 745 199.6 115.2 26.7 20 B MET O 745 199.3 114.1 27.2 20 B GLU N 746 200.2 116.1 27.5 20 B GLU CA 746 200.6 115.8 28.9 21 B GLU CB 746 201.3 117.0 29.5 21 B GLU CG 746 201.6 116.9 30.9 23 B GLU CD 746 202.2 118.2 31.4 24 B GLU OE1 746 202.0 119.3 30.8 25 B GLU OE2 746 202.9 118.1 32.5 25 B GLU C 746 199.3 115.5 29.7 21 B GLU O 746 198.2 116.1 29.4 22 B ALA N 747 199.4 114.7 30.7 21 B ALA CA 747 198.2 114.4 31.5 21 B ALA CB 747 198.5 113.2 32.4 22 B ALA C 747 197.9 115.6 32.3 21 B ALA O 747 198.7 116.2 33.0 20 B HIS N 748 196.6 116.0 32.3 21 B HIS CA 748 196.0 117.1 33.0 20 B HIS CB 748 195.7 118.3 32.0 20 B HIS CG 748 195.6 119.6 32.6 20 B HIS CD2 748 196.6 120.6 32.7 21 B HIS ND1 748 194.5 120.1 33.2 20 B HIS CE1 748 194.7 121.3 33.7 20 B HIS NE2 748 196.0 121.6 33.4 21 B HIS C 748 194.8 116.8 33.8 20 B HIS O 748 193.9 116.0 33.3 21 B GLY N 749 194.6 117.4 35.0 20 B GLY CA 749 193.5 117.1 35.8 18 B GLY C 749 192.1 117.5 35.2 18 B GLY O 749 191.2 116.8 35.3 20 B GLY N 750 192.0 118.7 34.7 17 B GLY CA 750 190.8 119.1 34.1 15 B GLY C 750 190.3 118.2 33.0 16 B GLY O 750 189.1 117.9 32.9 15 B TYR N 751 191.2 117.8 32.1 16 B TYR CA 751 190.8 116.9 31.0 17 B TYR CB 751 191.9 116.9 30.0 15 B TYR CG 751 192.0 118.1 29.2 15 B TYR CD1 751 193.2 118.9 29.3 15 B TYR CE1 751 193.4 120.1 28.6 15 B TYR CD2 751 191.0 118.6 28.4 15 B TYR CE2 751 191.1 119.8 27.6 16 B TYR CZ 751 192.3 120.5 27.7 16 B TYR OH 751 192.5 121.7 27.0 17 B TYR C 751 190.6 115.5 31.6 19 B TYR O 751 189.6 114.8 31.1 20 B THR N 752 191.4 115.0 32.5 18 B THR CA 752 191.3 113.7 33.1 18 B THR CB 752 192.4 113.5 34.1 18 B THR OG1 752 193.6 113.6 33.5 19 B THR CG2 752 192.3 112.1 34.7 18 B THR C 752 189.9 113.5 33.8 19 B THR O 752 189.4 112.4 33.9 21 B PHE N 753 189.3 114.6 34.3 18 B PHE CA 753 188.0 114.5 34.9 17 B PHE CB 753 187.6 115.7 35.7 16 B PHE CG 753 186.2 115.7 36.2 16 B PHE CD1 753 185.8 114.9 37.2 16 B PHE CD2 753 185.3 116.5 35.5 16 B PHE CE1 753 184.4 114.8 37.6 15 B PHE CE2 753 183.9 116.4 35.8 16 B PHE CZ 753 183.5 115.6 36.9 16 B PHE C 753 186.9 114.4 33.7 17 B PHE O 753 186.0 113.7 33.8 17 B CYS N 754 187.1 115.2 32.7 17 B CYS CA 754 186.2 115.1 31.5 18 B CYS CB 754 186.6 116.1 30.5 18 B CYS SG 754 186.4 117.8 30.9 18 B CYS C 754 186.3 113.7 30.9 18 B CYS O 754 185.3 113.2 30.5 19 B GLY N 755 187.5 113.2 30.8 19 B GLY CA 755 187.7 111.9 30.2 19 B GLY C 755 187.0 110.8 31.0 20 B GLY O 755 186.1 110.2 30.5 21 B LEU N 756 187.4 110.6 32.3 20 B LEU CA 756 186.8 109.6 33.1 21 B LEU CB 756 187.4 109.6 34.5 20 B LEU CG 756 187.0 108.5 35.5 19 B LEU CD1 756 187.2 107.2 34.8 19 B LEU CD2 756 187.8 108.6 36.7 19 B LEU C 756 185.2 109.8 33.3 22 B LEU O 756 184.5 108.9 33.0 23 B ALA N 757 184.8 111.0 33.6 22 B ALA CA 757 183.3 111.2 33.8 21 B ALA CB 757 183.1 112.7 34.1 20 B ALA C 757 182.6 110.9 32.6 21 B ALA O 757 181.5 110.3 32.6 22 B ALA N 758 183.1 111.2 31.4 21 B ALA CA 758 182.4 110.9 30.2 20 B ALA CB 758 183.2 111.5 29.0 20 B ALA C 758 182.3 109.4 30.0 21 B ALA O 758 181.3 108.9 29.6 22 B LEU N 759 183.4 108.6 30.3 21 B LEU CA 759 183.4 107.2 30.2 21 B LEU CB 759 184.8 106.6 30.4 20 B LEU CG 759 185.8 106.8 29.3 20 B LEU CD1 759 187.1 106.2 29.6 19 B LEU CD2 759 185.3 106.2 28.0 19 B LEU C 759 182.3 106.6 31.2 22 B LEU O 759 181.5 105.8 30.8 23 B VAL N 760 182.4 107.1 32.4 21 B VAL CA 760 181.4 106.6 33.4 20 B VAL CB 760 181.5 107.4 34.7 20 B VAL CG1 760 180.4 107.1 35.6 20 B VAL CG2 760 182.8 107.1 35.4 20 B VAL C 760 180.0 106.8 32.9 21 B VAL O 760 179.2 105.9 33.0 23 B ILE N 761 179.8 107.9 32.2 22 B ILE CA 761 178.5 108.1 31.6 24 B ILE CB 761 178.4 109.5 31.0 23 B ILE CG2 761 177.0 109.8 30.4 23 B ILE CG1 761 178.6 110.6 32.1 22 B ILE CD1 761 178.5 112.0 31.6 22 B ILE C 761 178.2 107.1 30.5 26 B ILE O 761 177.1 106.5 30.3 26 B LEU N 762 179.2 106.8 29.7 28 B LEU CA 762 179.1 105.8 28.6 30 B LEU CB 762 180.2 106.2 27.5 28 B LEU CG 762 180.0 107.5 26.8 27 B LEU CD1 762 181.2 107.6 25.8 26 B LEU CD2 762 178.7 107.6 26.0 26 B LEU C 762 179.3 104.4 29.1 31 B LEU O 762 179.2 103.4 28.3 30 B LYS N 763 179.5 104.2 30.4 33 B LYS CA 763 179.7 103.0 31.1 35 B LYS CB 763 178.4 102.1 31.0 37 B LYS CG 763 177.2 102.7 31.5 40 B LYS CD 763 176.0 102.3 30.6 41 B LYS CE 763 174.7 102.6 31.2 42 B LYS NZ 763 173.6 102.0 30.4 44 B LYS C 763 180.8 102.2 30.4 36 B LYS O 763 180.7 101.1 30.0 37 B LYS N 764 181.9 102.9 30.2 35 B LYS CA 764 183.1 102.3 29.6 35 B LYS CB 764 183.3 102.8 28.2 35 B LYS CG 764 182.2 102.5 27.2 36 B LYS CD 764 182.0 101.1 27.1 37 B LYS CE 764 181.1 100.8 25.9 38 B LYS NZ 764 180.0 101.8 25.8 39 B LYS C 764 184.4 102.5 30.3 36 B LYS O 764 185.5 102.4 29.8 36 B GLU N 765 184.3 102.9 31.6 37 B GLU CA 765 185.5 103.2 32.4 39 B GLU CB 765 185.2 103.2 33.9 39 B GLU CG 765 183.8 103.8 34.3 41 B GLU CD 765 182.8 102.8 34.5 42 B GLU OE1 765 182.7 102.3 35.6 43 B GLU OE2 765 182.0 102.5 33.5 43 B GLU C 765 186.6 102.2 32.2 39 B GLU O 765 187.7 102.5 32.3 38 B ARG N 766 186.2 100.9 32.0 40 B ARG CA 766 187.1  99.8 31.8 41 B ARG CB 766 186.4  98.5 31.7 44 B ARG CG 766 186.1  97.9 33.0 48 B ARG CD 766 184.6  98.2 33.5 51 B ARG NE 766 184.6  98.7 34.9 54 B ARG CZ 766 183.5  99.1 35.5 55 B ARG NH1 766 183.6  99.5 36.8 55 B ARG NH2 766 182.3  99.1 34.9 55 B ARG C 766 188.1 100.1 30.6 40 B ARG O 766 189.2  99.5 30.6 40 B SER N 767 187.7 100.9 29.7 39 B SER CA 767 188.5 101.3 28.5 38 B SER CB 767 187.8 102.2 27.6 38 B SER OG 767 186.6 101.6 27.1 39 B SER C 767 189.8 101.9 28.9 37 B SER O 767 190.7 102.1 28.1 38 B LEU N 768 190.0 102.4 30.2 36 B LEU CA 768 191.2 103.0 30.6 36 B LEU CB 768 190.8 104.4 31.3 35 B LEU CG 768 190.1 105.5 30.6 35 B LEU CD1 768 189.8 106.6 31.6 34 B LEU CD2 768 191.1 106.0 29.5 35 B LEU C 768 191.9 102.2 31.7 35 B LEU O 768 191.2 101.6 32.5 37 B ASN N 769 193.2 102.3 31.7 34 B ASN CA 769 193.9 101.5 32.7 33 B ASN CB 769 195.4 101.6 32.5 33 B ASN CG 769 196.2 100.9 33.6 33 B ASN OD1 769 195.8 100.8 34.7 34 B ASN ND2 769 197.4 100.4 33.2 34 B ASN C 769 193.6 102.3 34.0 33 B ASN O 769 194.2 103.3 34.3 34 B LEU N 770 192.7 101.7 34.8 31 B LEU CA 770 192.3 102.4 36.0 30 B LEU CB 770 190.9 101.8 36.5 29 B LEU CG 770 189.8 102.1 35.5 28 B LEU CD1 770 188.5 101.9 36.3 28 B LEU CD2 770 189.8 103.4 34.9 29 B LEU C 770 193.3 102.3 37.1 30 B LEU O 770 193.2 103.1 38.1 30 B LYS N 771 194.3 101.5 37.0 32 B LYS CA 771 195.3 101.5 38.1 35 B LYS CB 771 196.0 100.1 38.2 38 B LYS CG 771 195.3  99.2 39.2 43 B LYS CD 771 194.9  99.9 40.5 45 B LYS CE 771 194.0  99.1 41.5 47 B LYS NZ 771 192.6  98.8 41.0 46 B LYS C 771 196.3 102.6 37.9 35 B LYS O 771 196.6 103.3 38.9 35 B SER N 772 196.8 102.7 36.7 35 B SER CA 772 197.8 103.7 36.4 35 B SER CB 772 198.3 103.7 35.0 35 B SER OG 772 197.3 103.5 34.1 35 B SER C 772 197.1 105.1 36.7 35 B SER O 772 197.7 106.0 37.3 37 B LEU N 773 195.9 105.2 36.2 34 B LEU CA 773 195.2 106.4 36.4 33 B LEU CB 773 193.8 106.3 35.6 33 B LEU CG 773 192.7 107.3 36.0 33 B LEU CD1 773 193.1 108.7 36.2 33 B LEU CD2 773 191.6 107.1 35.0 34 B LEU C 773 195.0 106.6 37.9 34 B LEU O 773 195.3 107.7 38.3 34 B LEU N 774 194.6 105.6 38.6 33 B LEU CA 774 194.4 105.8 40.1 33 B LEU CB 774 194.1 104.5 40.7 34 B LEU CG 774 194.2 104.5 42.3 34 B LEU CD1 774 193.1 105.5 42.8 33 B LEU CD2 774 193.9 103.1 42.9 34 B LEU C 774 195.7 106.3 40.7 32 B LEU O 774 195.7 107.2 41.5 31 B GLN N 775 196.8 105.8 40.2 33 B GLN CA 775 198.1 106.2 40.7 34 B GLN CB 775 199.2 105.2 40.2 35 B GLN CG 775 200.6 105.6 40.8 39 B GLN CD 775 201.6 104.5 40.6 42 B GLN OE1 775 202.4 104.2 41.6 43 B GLN NE2 775 201.7 103.9 39.4 43 B GLN C 775 198.5 107.6 40.5 33 B GLN O 775 198.9 108.3 41.4 34 B TRP N 776 198.2 108.1 39.2 31 B TRP CA 776 198.5 109.5 38.9 29 B TRP CB 776 198.5 109.6 37.4 28 B TRP CG 776 198.6 111.0 36.9 26 B TRP CD2 776 197.5 111.9 36.6 26 B TRP CE2 776 198.0 113.0 36.0 26 B TRP CE3 776 196.1 111.7 36.8 26 B TRP CD1 776 199.7 111.7 36.5 26 B TRP NE1 776 199.3 112.9 36.0 26 B TRP CZ2 776 197.2 114.1 35.7 26 B TRP CZ3 776 195.3 112.8 36.4 26 B TRP CH2 776 195.8 114.0 35.8 26 B TRP C 776 197.7 110.5 39.6 28 B TRP O 776 198.2 111.4 40.3 27 B VAL N 777 196.3 110.3 39.7 27 B VAL CA 777 195.5 111.3 40.4 26 B VAL CB 777 193.9 110.8 40.3 26 B VAL CG1 777 193.7 109.6 41.0 26 B VAL CG2 777 193.1 111.9 40.8 25 B VAL C 777 195.9 111.4 41.8 27 B VAL O 777 195.9 112.5 42.3 26 B THR N 778 196.2 110.3 42.5 27 B THR CA 778 196.6 110.4 43.9 27 B THR CB 778 196.8 109.0 44.5 26 B THR OG1 778 197.8 108.2 43.8 25 B THR CG2 778 195.4 108.2 44.3 26 B THR C 778 198.0 111.1 44.0 27 B THR O 778 198.3 111.7 45.1 28 B SER N 779 198.8 111.1 43.0 27 B SER CA 779 200.1 111.8 43.1 28 B SER CB 779 201.0 111.2 42.0 28 B SER OG 779 201.1 109.8 42.1 28 B SER C 779 199.9 113.3 42.9 29 B SER O 779 200.8 114.1 43.2 30 B ARG N 780 198.7 113.7 42.4 28 B ARG CA 780 198.5 115.1 42.1 27 B ARG CB 780 197.4 115.3 41.1 27 B ARG CG 780 197.6 114.6 39.8 26 B ARG CD 780 198.7 115.3 38.9 24 B ARG NE 780 200.0 115.3 39.4 22 B ARG CZ 780 200.8 114.3 39.5 23 B ARG NH1 780 200.4 113.1 39.0 24 B ARG NH2 780 202.0 114.4 40.0 23 B ARG C 780 198.2 115.9 43.4 28 B ARG O 780 198.1 117.1 43.4 29 B GLN N 781 198.0 115.2 44.5 29 B GLN CA 781 197.7 115.9 45.8 30 B GLN CB 781 196.9 115.0 46.8 31 B GLN CG 781 196.6 115.8 48.1 31 B GLN CD 781 195.5 115.2 48.9 31 B GLN OE1 781 195.4 114.0 49.1 31 B GLN NE2 781 194.6 116.1 49.4 31 B GLN C 781 199.0 116.3 46.3 31 B GLN O 781 199.9 115.5 46.4 31 B MET N 782 199.2 117.6 46.7 31 B MET CA 782 200.4 118.1 47.2 32 B MET CB 782 200.4 119.6 47.0 31 B MET CG 782 200.1 120.1 45.6 30 B MET SD 782 201.3 119.5 44.3 30 B MET CE 782 202.7 120.3 44.9 29 B MET C 782 200.6 117.9 48.7 33 B MET O 782 199.8 118.3 49.5 33 B ARG N 783 201.6 117.1 49.1 34 B ARG CA 783 202.0 116.8 50.5 36 B ARG CB 783 203.3 116.0 50.5 37 B ARG CG 783 204.4 116.8 50.0 40 B ARG CD 783 205.4 115.9 49.2 42 B ARG NE 783 205.9 114.9 50.1 45 B ARG CZ 783 206.2 113.6 49.7 47 B ARG NH1 783 206.0 113.3 48.4 48 B ARG NH2 783 206.6 112.8 50.6 48 B ARG C 783 202.0 117.9 51.5 35 B ARG O 783 201.7 117.7 52.7 35 B PHE N 784 202.5 119.1 51.1 35 B PHE CA 784 202.6 120.2 52.0 34 B PHE CB 784 203.8 121.1 51.6 34 B PHE CG 784 204.1 122.1 52.7 34 B PHE CD1 784 204.9 121.8 53.7 34 B PHE CD2 784 203.5 123.4 52.6 34 B PHE CE1 784 205.1 122.8 54.7 35 B PHE CE2 784 203.7 124.3 53.6 34 B PHE CZ 784 204.5 124.0 54.6 34 B PHE C 784 201.3 121.1 52.0 33 B PHE O 784 200.8 121.4 53.0 34 B GLU N 785 200.9 121.5 50.8 32 B GLU CA 785 199.8 122.4 50.7 31 B GLU CB 785 199.8 123.1 49.3 31 B GLU CG 785 201.0 123.9 49.0 31 B GLU CD 785 202.1 123.0 48.2 32 B GLU OE1 785 202.0 123.0 46.9 33 B GLU OE2 785 203.0 122.5 48.8 32 B GLU C 785 198.5 121.7 51.0 31 B GLU O 785 197.5 122.2 51.4 31 B GLY N 786 198.5 120.4 50.6 30 B GLY CA 786 197.3 119.6 50.8 28 B GLY C 786 196.3 119.7 49.7 27 B GLY O 786 195.3 118.9 49.6 27 B GLY N 787 196.4 120.7 48.9 26 B GLY CA 787 195.5 120.9 47.7 24 B GLY C 787 196.1 120.1 46.6 23 B GLY O 787 197.2 119.5 46.7 22 B PHE N 788 195.4 120.1 45.4 22 B PHE CA 788 195.8 119.4 44.2 23 B PHE CB 788 194.5 118.7 43.6 22 B PHE CG 788 194.3 117.3 44.2 23 B PHE CD1 788 193.4 117.2 45.3 23 B PHE CD2 788 194.9 116.2 43.8 23 B PHE CE1 788 193.1 116.0 45.9 23 B PHE CE2 788 194.7 114.9 44.3 24 B PHE CZ 788 193.8 114.8 45.4 23 B PHE C 788 196.4 120.3 43.2 23 B PHE O 788 196.3 121.5 43.1 24 B GLN N 789 197.3 119.6 42.3 22 B GLN CA 789 198.0 120.3 41.3 23 B GLN CB 789 199.5 120.0 41.3 23 B GLN CG 789 199.8 118.5 41.1 23 B GLN CD 789 201.3 118.3 41.0 24 B GLN OE1 789 201.8 117.2 40.7 23 B GLN NE2 789 202.1 119.3 41.2 25 B GLN C 789 197.4 119.9 40.0 23 B GLN O 789 196.9 118.8 39.8 24 B GLY N 790 197.4 120.8 39.0 24 B GLY CA 790 196.8 120.4 37.7 22 B GLY C 790 197.5 119.3 37.0 21 B GLY O 790 196.9 118.4 36.4 20 B ARG N 791 198.9 119.3 36.9 20 B ARG CA 791 199.6 118.3 36.2 20 B ARG CB 791 199.9 118.7 34.8 20 B ARG CG 791 199.5 120.2 34.5 20 B ARG CD 791 199.9 120.5 33.0 20 B ARG NE 791 199.8 122.0 32.9 21 B ARG CZ 791 200.2 122.7 31.8 21 B ARG NH1 791 200.9 122.1 30.9 22 B ARG NH2 791 200.1 124.0 31.8 21 B ARG C 791 201.0 118.2 37.0 22 B ARG O 791 201.3 119.2 37.6 22 B CYS N 792 201.6 117.1 36.9 22 B CYS CA 792 202.9 116.9 37.6 23 B CYS CB 792 203.6 115.6 37.0 23 B CYS SG 792 205.1 115.2 37.9 24 B CYS C 792 203.9 118.1 37.5 24 B CYS O 792 203.9 118.8 36.5 26 B ASN N 793 204.6 118.4 38.6 24 B ASN CA 793 205.6 119.5 38.6 25 B ASN CB 793 206.8 119.2 37.7 25 B ASN CG 793 207.9 118.5 38.5 25 B ASN OD1 793 207.9 118.6 39.7 26 B ASN ND2 793 208.9 117.9 37.8 24 B ASN C 793 205.0 120.8 38.2 24 B ASN O 793 205.6 121.7 37.5 23 B LYS N 794 203.8 121.0 38.7 24 B LYS CA 794 203.0 122.3 38.5 24 B LYS CB 794 201.7 122.0 37.7 24 B LYS CG 794 201.6 122.9 36.5 25 B LYS CD 794 202.7 122.8 35.6 25 B LYS CE 794 202.4 123.7 34.4 26 B LYS NZ 794 202.0 125.1 34.6 25 B LYS C 794 202.6 122.7 39.9 25 B LYS O 794 203.1 122.2 40.9 26 B LEU N 795 201.8 123.8 40.0 24 B LEU CA 795 201.4 124.3 41.3 24 B LEU CB 795 201.5 125.9 41.3 23 B LEU CG 795 202.8 126.5 41.0 21 B LEU CD1 795 202.7 128.0 41.2 19 B LEU CD2 795 204.0 125.9 41.7 20 B LEU C 795 200.0 123.9 41.8 24 B LEU O 795 199.2 123.4 41.0 25 B VAL N 796 199.8 124.2 43.1 24 B VAL CA 796 198.5 123.9 43.7 24 B VAL CB 796 198.5 124.1 45.2 25 B VAL CG1 796 198.1 122.8 45.9 27 B VAL CG2 796 199.8 124.6 45.7 25 B VAL C 796 197.5 124.8 43.1 23 B VAL O 796 197.8 125.9 42.7 24 B ASP N 797 196.2 124.5 43.2 20 B ASP CA 797 195.1 125.4 42.8 18 B ASP CB 797 195.1 125.5 41.2 16 B ASP CG 797 194.0 126.4 40.7 15 B ASP OD1 797 193.0 126.7 41.3 16 B ASP OD2 797 194.1 126.8 39.5 15 B ASP C 797 193.8 124.9 43.3 19 B ASP O 797 193.4 123.7 43.0 19 B GLY N 798 193.0 125.7 43.9 19 B GLY CA 798 191.7 125.4 44.4 19 B GLY C 798 190.7 124.6 43.4 20 B GLY O 798 190.2 123.6 43.9 21 B CYS N 799 190.6 125.0 42.2 21 B CYS CA 799 189.6 124.3 41.3 22 B CYS CB 799 189.4 125.0 40.0 23 B CYS SG 799 190.9 125.3 39.0 25 B CYS C 799 189.9 122.9 41.2 24 B CYS O 799 189.0 122.1 40.9 25 B TYR N 800 191.2 122.5 41.3 25 B TYR CA 800 191.6 121.2 41.2 26 B TYR CB 800 193.1 121.0 41.0 26 B TYR CG 800 193.5 121.6 39.6 27 B TYR CD1 800 194.7 122.3 39.5 27 B TYR CE1 800 195.0 122.8 38.3 28 B TYR CD2 800 192.8 121.3 38.5 27 B TYR CE2 800 193.1 121.8 37.3 28 B TYR CZ 800 194.3 122.6 37.2 28 B TYR OH 800 194.6 123.2 36.0 30 B TYR C 800 191.2 120.3 42.4 28 B TYR O 800 191.4 119.1 42.4 30 B SER N 801 190.6 121.0 43.4 27 B SER CA 801 190.2 120.3 44.5 26 B SER CB 801 189.7 121.3 45.6 26 B SER OG 801 190.8 122.1 45.9 25 B SER C 801 189.0 119.4 44.0 27 B SER O 801 188.6 118.4 44.6 28 B PHE N 802 188.4 119.9 42.9 26 B PHE CA 802 187.2 119.2 42.3 25 B PHE CB 802 186.1 120.0 41.8 24 B PHE CG 802 185.1 119.2 41.1 23 B PHE CD1 802 184.0 118.6 41.7 23 B PHE CD2 802 185.1 119.1 39.7 23 B PHE CE1 802 183.1 117.8 41.0 23 B PHE CE2 802 184.2 118.4 39.0 22 B PHE CZ 802 183.2 117.7 39.7 22 B PHE C 802 187.6 118.3 41.1 26 B PHE O 802 187.3 117.2 41.0 28 B TRP N 803 188.3 118.9 40.1 24 B TRP CA 803 188.7 118.2 38.9 22 B TRP CB 803 189.4 119.1 37.9 20 B TRP CG 803 188.6 120.4 37.5 19 B TRP CD2 803 187.4 120.5 36.7 19 B TRP CE2 803 187.2 121.9 36.5 19 B TRP CE3 803 186.5 119.6 36.2 20 B TRP CD1 803 189.0 121.7 37.7 19 B TRP NE1 803 188.2 122.5 37.1 19 B TRP CZ2 803 186.1 122.3 35.8 19 B TRP CZ3 803 185.4 120.0 35.5 20 B TRP CH2 803 185.2 121.4 35.3 20 B TRP C 803 189.6 117.0 39.2 22 B TRP O 803 189.5 116.0 38.5 23 B GLN N 804 190.5 117.2 40.2 22 B GLN CA 804 191.4 116.1 40.6 22 B GLN CB 804 192.7 116.6 41.2 21 B GLN CG 804 193.6 117.4 40.2 22 B GLN CD 804 194.2 116.5 39.2 23 B GLN OE1 804 193.6 115.5 38.8 25 B GLN NE2 804 195.3 116.9 38.7 23 B GLN C 804 190.7 115.2 41.6 23 B GLN O 804 190.4 114.1 41.3 25 B ALA N 805 190.5 115.7 42.8 23 B ALA CA 805 189.9 115.0 43.9 22 B ALA CB 805 189.7 115.9 45.1 22 B ALA C 805 188.6 114.4 43.5 22 B ALA O 805 188.2 113.3 44.0 22 B GLY N 806 187.9 115.1 42.6 21 B GLY CA 806 186.6 114.5 42.1 22 B GLY C 806 186.8 113.2 41.4 24 B GLY O 806 185.8 112.4 41.3 24 B LEU N 807 188.0 112.9 40.9 25 B LEU CA 807 188.2 111.6 40.2 27 B LEU CB 807 189.5 111.6 39.5 26 B LEU CG 807 189.8 112.4 38.2 26 B LEU CD1 807 191.3 112.6 38.0 27 B LEU CD2 807 189.1 111.8 37.0 25 B LEU C 807 188.1 110.4 41.1 28 B LEU O 807 187.8 109.3 40.7 28 B LEU N 808 188.3 110.7 42.4 28 B LEU CA 808 188.2 109.6 43.4 30 B LEU CB 808 188.9 109.9 44.7 30 B LEU CG 808 190.4 109.9 44.2 30 B LEU CD1 808 191.2 110.9 44.9 31 B LEU CD2 808 191.0 108.6 44.3 31 B LEU C 808 186.8 109.0 43.5 30 B LEU O 808 186.7 107.7 43.6 33 B PRO N 809 185.8 109.8 43.7 30 B PRO CD 809 185.7 111.2 44.0 30 B PRO CA 809 184.5 109.2 43.8 30 B PRO CB 809 183.5 110.4 43.8 30 B PRO CG 809 184.3 111.3 44.6 30 B PRO C 809 184.2 108.3 42.5 30 B PRO O 809 183.8 107.2 42.6 31 B LEU N 810 184.7 108.8 41.4 31 B LEU CA 810 184.5 108.1 40.1 30 B LEU CB 810 185.0 109.0 39.0 28 B LEU CG 810 184.1 110.2 38.7 27 B LEU CD1 810 184.5 111.0 37.5 26 B LEU CD2 810 182.7 109.7 38.6 26 B LEU C 810 185.3 106.8 40.0 32 B LEU O 810 184.7 105.8 39.6 32 B LEU N 811 186.5 106.8 40.5 33 B LEU CA 811 187.3 105.6 40.5 35 B LEU CB 811 188.8 105.9 40.8 33 B LEU CG 811 189.6 106.4 39.7 32 B LEU CD1 811 190.9 106.7 40.2 31 B LEU CD2 811 189.6 105.4 38.6 30 B LEU C 811 186.8 104.6 41.5 38 B LEU O 811 187.0 103.4 41.3 39 B HIS N 812 186.2 105.1 42.6 40 B HIS CA 812 185.6 104.2 43.6 41 B HIS CB 812 185.0 105.0 44.7 42 B HIS CG 812 185.1 104.3 46.1 42 B HIS CD2 812 184.4 103.4 46.7 42 B HIS ND1 812 186.2 104.5 46.9 43 B HIS CE1 812 186.1 103.8 48.0 42 B HIS NE2 812 185.0 103.0 47.9 42 B HIS C 812 184.5 103.3 42.9 42 B HIS O 812 184.6 102.1 42.9 42 B ARG N 813 183.5 104.0 42.3 44 B ARG CA 813 182.5 103.3 41.5 46 B ARG CB 813 181.7 104.2 40.6 49 B ARG CG 813 180.6 105.0 41.2 52 B ARG CD 813 180.1 106.1 40.2 55 B ARG NE 813 179.0 106.9 40.8 57 B ARG CZ 813 179.1 107.8 41.8 58 B ARG NH1 813 180.2 107.9 42.5 59 B ARG NH2 813 178.0 108.5 42.2 59 B ARG C 813 183.1 102.2 40.6 46 B ARG O 813 183.0 101.0 40.9 47 B ALA N 814 183.8 102.7 39.6 45 B ALA CA 814 184.5 101.8 38.7 45 B ALA CB 814 185.4 102.6 37.8 45 B ALA C 814 185.2 100.6 39.3 45 B ALA O 814 184.9  99.5 39.0 45 B LEU N 815 186.1 100.9 40.2 46 B LEU CA 815 186.9  99.8 40.9 47 B LEU CB 815 187.9 100.3 41.9 47 B LEU CG 815 189.1 101.1 41.3 47 B LEU CD1 815 190.1 101.5 42.3 48 B LEU CD2 815 189.8 100.2 40.2 47 B LEU C 815 185.9  98.8 41.6 48 B LEU O 815 185.9  97.6 41.3 49 B HIS N 816 185.0  99.4 42.4 49 B HIS CA 816 184.1  98.6 43.1 51 B HIS CB 816 183.3  99.5 44.1 53 B HIS CG 816 182.3  98.7 44.8 54 B HIS CD2 816 182.3  97.9 45.8 55 B HIS ND1 816 180.9  98.8 44.4 55 B HIS CE1 816 180.2  98.0 45.2 56 B HIS NE2 816 181.0  97.5 46.1 56 B HIS C 816 183.1  97.8 42.2 52 B HIS O 816 182.6  96.8 42.7 52 B ALA N 817 182.9  98.3 41.0 52 B ALA CA 817 182.0  97.6 40.1 52 B ALA CB 817 181.6  98.5 39.0 52 B ALA C 817 182.7  96.3 39.6 53 B ALA O 817 182.1  95.5 39.0 53 B GLN N 818 184.0  96.2 39.8 54 B GLN CA 818 184.7  95.1 39.4 55 B GLN CB 818 186.1  95.5 38.8 55 B GLN CG 818 185.8  96.4 37.6 56 B GLN CD 818 187.1  97.2 37.2 56 B GLN OE1 818 188.2  96.8 37.5 57 B GLN NE2 818 186.9  98.3 36.6 57 B GLN C 818 185.0  94.4 40.8 55 B GLN O 818 186.0  93.7 41.0 55 B GLY N 819 184.1  94.6 41.7 55 B GLY CA 819 184.1  94.0 43.0 56 B GLY C 819 185.5  94.1 43.7 57 B GLY O 819 186.0  93.1 44.1 57 B ASP N 820 186.1  95.2 43.6 57 B ASP CA 820 187.4  95.3 44.3 57 B ASP CB 820 188.1  96.7 44.0 57 B ASP CG 820 189.6  96.7 44.0 57 B ASP OD1 820 190.2  96.9 43.0 57 B ASP OD2 820 190.2  96.5 45.1 56 B ASP C 820 187.2  95.1 45.7 57 B ASP O 820 186.2  95.6 46.3 57 B PRO N 821 187.9  94.2 46.4 57 B PRO CD 821 188.7  93.2 45.7 57 B PRO CA 821 187.7  93.9 47.8 57 B PRO CB 821 188.3  92.5 47.9 57 B PRO CG 821 189.4  92.5 46.9 57 B PRO C 821 188.4  94.9 48.7 58 B PRO O 821 187.9  95.3 49.7 59 B ALA N 822 189.6  95.4 48.3 56 B ALA CA 822 190.4  96.3 49.1 55 B ALA CB 822 191.9  96.3 48.6 54 B ALA C 822 189.9  97.8 49.2 54 B ALA O 822 190.6  98.6 49.8 53 B LEU N 823 188.8  98.1 48.7 54 B LEU CA 823 188.2  99.5 48.7 54 B LEU CB 823 187.2  99.7 47.6 54 B LEU CG 823 187.6  99.7 46.2 54 B LEU CD1 823 186.5 100.0 45.3 53 B LEU CD2 823 188.8 100.7 46.0 54 B LEU C 823 187.6  99.8 50.0 55 B LEU O 823 186.6  99.2 50.5 55 B SER N 824 188.0 101.0 50.6 55 B SER CA 824 187.5 101.4 51.9 55 B SER CB 824 188.2 102.7 52.3 55 B SER OG 824 187.7 103.2 53.6 55 B SER C 824 186.0 101.7 51.8 56 B SER O 824 185.3 102.0 50.8 56 B MET N 825 185.4 101.5 53.0 58 B MET CA 825 183.9 101.7 53.2 59 B MET CB 825 183.3 100.5 53.9 61 B MET CG 825 183.2  99.2 53.1 63 B MET SD 825 182.3  99.4 51.5 66 B MET CE 825 183.4  98.2 50.4 66 B MET C 825 183.7 103.0 54.0 59 B MET O 825 182.7 103.0 54.7 59 B SER N 826 184.6 103.9 53.9 58 B SER CA 826 184.4 105.2 54.6 57 B SER CB 826 184.9 105.0 56.1 57 B SER OG 826 186.2 104.5 56.1 57 B SER C 826 185.1 106.4 54.0 56 B SER O 826 184.6 107.6 54.2 56 B HIS N 827 186.2 106.3 53.3 54 B HIS CA 827 186.9 107.4 52.7 51 B HIS CB 827 188.1 107.8 53.6 53 B HIS CG 827 187.9 107.9 55.0 54 B HIS CD2 827 188.3 107.2 56.1 54 B HIS ND1 827 187.1 109.0 55.6 55 B HIS CE1 827 187.1 108.9 56.9 55 B HIS NE2 827 187.8 107.9 57.2 55 B HIS C 827 187.5 107.2 51.3 48 B HIS O 827 187.9 106.1 51.0 48 B TRP N 828 187.5 108.3 50.5 45 B TRP CA 828 188.0 108.3 49.2 40 B TRP CB 828 187.7 109.6 48.5 36 B TRP CG 828 186.3 109.9 48.6 33 B TRP CD2 828 185.2 109.2 48.0 32 B TRP CE2 828 184.1 109.9 48.3 32 B TRP CE3 828 185.1 107.9 47.4 32 B TRP CD1 828 185.8 111.0 49.1 33 B TRP NE1 828 184.4 111.1 48.9 32 B TRP CZ2 828 182.8 109.5 47.9 32 B TRP CZ3 828 183.9 107.5 47.0 32 B TRP CH2 828 182.7 108.3 47.2 32 B TRP C 828 189.5 108.1 49.3 40 B TRP O 828 190.1 108.4 50.3 40 B MET N 829 190.1 107.7 48.2 40 B MET CA 829 191.6 107.4 48.2 39 B MET CB 829 191.9 106.3 47.2 39 B MET CG 829 191.1 105.0 47.4 40 B MET SD 829 191.6 103.6 46.4 41 B MET CE 829 193.4 103.7 46.6 40 B MET C 829 192.4 108.7 48.1 39 B MET O 829 193.1 108.8 47.1 39 B PHE N 830 192.3 109.5 49.1 38 B PHE CA 830 193.1 110.8 49.1 36 B PHE CB 830 192.7 111.8 48.0 33 B PHE CG 830 191.4 112.6 48.2 29 B PHE CD1 830 191.5 113.8 49.0 28 B PHE CD2 830 190.3 112.2 47.6 28 B PHE CE1 830 190.3 114.5 49.1 28 B PHE CE2 830 189.1 113.0 47.7 28 B PHE CZ 830 189.2 114.2 48.5 28 B PHE C 830 192.9 111.4 50.5 37 B PHE O 830 191.9 111.1 51.2 38 B HIS N 831 193.8 112.2 50.9 37 B HIS CA 831 193.7 112.9 52.2 37 B HIS CB 831 195.0 113.5 52.6 36 B HIS CG 831 195.2 113.6 54.1 36 B HIS CD2 831 194.5 114.3 55.1 36 B HIS ND1 831 196.3 113.0 54.7 36 B HIS CE1 831 196.3 113.3 56.0 36 B HIS NE2 831 195.2 114.0 56.3 36 B HIS C 831 192.6 113.9 52.2 38 B HIS O 831 192.8 115.0 51.7 39 B GLN N 832 191.4 113.6 52.6 38 B GLN CA 832 190.2 114.5 52.6 38 B GLN CB 832 188.9 113.8 53.0 37 B GLN CG 832 188.6 112.6 52.1 36 B GLN CD 832 187.5 111.8 52.6 35 B GLN OE1 832 186.6 112.2 53.3 34 B GLN NE2 832 187.6 110.5 52.3 34 B GLN C 832 190.4 115.7 53.6 39 B GLN O 832 189.9 116.8 53.4 38 B GLN N 833 191.1 115.4 54.7 41 B GLN CA 833 191.3 116.3 55.8 42 B GLN CB 833 192.0 115.7 57.0 43 B GLN CG 833 191.9 116.5 58.2 44 B GLN CD 833 193.0 116.1 59.2 45 B GLN OE1 833 193.8 115.2 59.0 45 B GLN NE2 833 193.1 116.9 60.3 45 B GLN C 833 192.2 117.5 55.2 41 B GLN O 833 191.9 118.6 55.4 41 B ALA N 834 193.3 117.1 54.6 40 B ALA CA 834 194.2 118.1 54.0 39 B ALA CB 834 195.4 117.4 53.4 38 B ALA C 834 193.5 118.9 53.0 38 B ALA O 834 193.5 120.1 53.0 39 B LEU N 835 192.8 118.3 52.0 37 B LEU CA 835 192.1 119.0 51.0 37 B LEU CB 835 191.4 118.1 50.0 36 B LEU CG 835 190.6 118.9 49.0 36 B LEU CD1 835 191.5 119.9 48.3 36 B LEU CD2 835 190.0 117.9 47.9 36 B LEU C 835 191.1 120.1 51.6 37 B LEU O 835 191.1 121.2 51.2 37 B GLN N 836 190.4 119.7 52.7 37 B GLN CA 836 189.5 120.6 53.4 37 B GLN CB 836 188.7 119.8 54.4 37 B GLN CG 836 187.5 119.1 53.8 38 B GLN CD 836 186.6 118.4 54.9 38 B GLN OE1 836 186.1 119.0 55.8 37 B GLN NE2 836 186.4 117.1 54.7 38 B GLN C 836 190.3 121.7 54.1 36 B GLN O 836 189.8 122.8 54.1 36 B GLU N 837 191.4 121.4 54.6 35 B GLU CA 837 192.2 122.4 55.3 36 B GLU CB 837 193.4 121.8 56.1 34 B GLU CG 837 192.8 121.1 57.3 34 B GLU CD 837 193.8 120.3 58.2 33 B GLU OE1 837 195.0 120.6 58.1 32 B GLU OE2 837 193.4 119.5 59.0 33 B GLU C 837 192.7 123.5 54.3 37 B GLU O 837 192.5 124.7 54.4 39 B TYR N 838 193.4 123.0 53.2 37 B TYR CA 838 193.9 124.0 52.2 35 B TYR CB 838 194.5 123.2 50.9 36 B TYR CG 838 194.9 124.1 49.8 37 B TYR CD1 838 196.1 124.9 49.8 36 B TYR CE1 838 196.4 125.8 48.8 35 B TYR CD2 838 194.0 124.3 48.7 36 B TYR CE2 838 194.3 125.2 47.7 35 B TYR CZ 838 195.5 126.0 47.7 35 B TYR OH 838 195.7 126.9 46.8 35 B TYR C 838 192.7 124.8 51.8 34 B TYR O 838 192.7 126.1 52.0 33 B ILE N 839 191.6 124.2 51.3 33 B ILE CA 839 190.4 124.9 50.8 31 B ILE CB 839 189.3 124.0 50.4 29 B ILE CG2 839 188.1 124.8 50.0 29 B ILE CG1 839 189.6 123.1 49.2 29 B ILE CD1 839 188.5 122.3 48.7 28 B ILE C 839 189.9 125.9 51.8 31 B ILE O 839 189.4 127.0 51.4 33 B LEU N 840 190.0 125.6 53.1 30 B LEU CA 840 189.5 126.5 54.1 29 B LEU CB 840 189.1 125.7 55.3 28 B LEU CG 840 187.8 124.9 55.2 28 B LEU CD1 840 187.8 124.0 56.4 28 B LEU CD2 840 186.6 125.9 55.2 27 B LEU C 840 190.6 127.6 54.6 29 B LEU O 840 190.2 128.8 54.7 30 B MET N 841 191.8 127.2 54.9 29 B MET CA 841 192.8 128.1 55.3 30 B MET CB 841 193.9 127.3 56.0 30 B MET CG 841 193.5 126.7 57.3 30 B MET SD 841 194.9 126.2 58.3 31 B MET CE 841 194.9 124.5 58.0 30 B MET C 841 193.4 128.9 54.2 31 B MET O 841 193.5 130.1 54.4 32 B CYS N 842 193.6 128.3 53.1 32 B CYS CA 842 194.2 129.0 52.0 31 B CYS CB 842 195.4 128.2 51.4 30 B CYS SG 842 196.5 127.7 52.7 31 B CYS C 842 193.4 129.6 50.8 32 B CYS O 842 193.8 130.6 50.3 33 B CYS N 843 192.3 129.0 50.5 33 B CYS CA 843 191.5 129.5 49.4 34 B CYS CB 843 191.2 128.3 48.4 33 B CYS SG 843 192.7 127.4 48.1 32 B CYS C 843 190.2 130.2 49.6 35 B CYS O 843 189.3 130.3 48.7 36 B GLN N 844 190.1 130.9 50.7 37 B GLN CA 844 188.9 131.6 51.0 39 B GLN CB 844 188.3 131.1 52.4 39 B GLN CG 844 186.9 131.4 52.6 38 B GLN CD 844 186.3 130.3 53.4 39 B GLN OE1 844 185.1 130.2 53.4 39 B GLN NE2 844 187.1 129.6 54.2 38 B GLN C 844 189.1 133.1 51.1 40 B GLN O 844 190.0 133.6 51.7 40 B CYS N 845 188.3 133.8 50.3 40 B CYS CA 845 188.5 135.3 50.3 41 B CYS CB 845 188.1 135.9 48.9 42 B CYS SG 845 187.9 137.7 48.9 42 B CYS C 845 187.5 135.9 51.4 42 B CYS O 845 186.3 135.6 51.4 43 B PRO N 846 188.1 136.7 52.3 42 B PRO CD 846 189.5 137.2 52.2 42 B PRO CA 846 187.4 137.3 53.4 42 B PRO CB 846 188.4 138.4 53.8 41 B PRO CG 846 189.7 137.8 53.6 41 B PRO C 846 186.1 137.9 53.0 42 B PRO O 846 185.0 137.6 53.5 43 B ALA N 847 186.1 138.8 51.9 41 B ALA CA 847 185.0 139.5 51.4 41 B ALA CB 847 185.4 140.7 50.5 41 B ALA C 847 183.9 138.6 50.6 40 B ALA O 847 183.0 139.2 50.1 40 B GLY N 848 184.2 137.3 50.5 39 B GLY CA 848 183.3 136.4 49.8 38 B GLY C 848 184.0 135.9 48.6 37 B GLY O 848 184.9 136.6 48.0 37 B GLY N 849 183.7 134.7 48.2 36 B GLY CA 849 184.4 134.1 47.0 33 B GLY C 849 185.6 133.3 47.5 32 B GLY O 849 186.1 133.5 48.6 32 B LEU N 850 185.8 132.2 46.7 31 B LEU CA 850 187.0 131.3 47.0 29 B LEU CB 850 186.6 129.9 47.0 28 B LEU CG 850 185.8 129.1 48.1 27 B LEU CD1 850 186.6 129.0 49.4 25 B LEU CD2 850 184.4 129.8 48.3 26 B LEU C 850 188.0 131.6 45.9 28 B LEU O 850 187.6 132.2 44.9 27 B LEU N 851 189.2 131.1 46.0 27 B LEU CA 851 190.2 131.4 45.0 27 B LEU CB 851 190.8 132.8 45.3 27 B LEU CG 851 191.2 133.1 46.8 26 B LEU CD1 851 192.5 132.4 47.2 26 B LEU CD2 851 191.2 134.6 46.9 26 B LEU C 851 191.2 130.4 44.8 28 B LEU O 851 191.4 129.5 45.6 29 B ASP N 852 192.0 130.5 43.6 28 B ASP CA 852 193.1 129.6 43.3 27 B ASP CB 852 193.9 130.3 42.2 28 B ASP CG 852 195.1 129.5 41.7 30 B ASP OD1 852 195.6 128.6 42.4 29 B ASP OD2 852 195.6 129.8 40.6 30 B ASP C 852 193.9 129.2 44.5 27 B ASP O 852 193.9 128.1 44.9 26 B LYS N 853 194.7 130.2 44.9 27 B LYS CA 853 195.6 130.0 46.0 27 B LYS CB 853 196.9 129.4 45.5 25 B LYS CG 853 197.7 130.4 44.7 24 B LYS CD 853 199.1 130.0 44.5 24 B LYS CE 853 199.2 128.7 43.8 24 B LYS NZ 853 198.6 128.7 42.5 23 B LYS C 853 195.8 131.4 46.6 28 B LYS O 853 195.4 132.4 45.9 26 B PRO N 854 196.4 131.5 47.8 31 B PRO CD 854 196.9 130.5 48.7 32 B PRO CA 854 196.6 132.9 48.3 32 B PRO CB 854 197.3 132.5 49.7 32 B PRO CG 854 198.0 131.2 49.5 32 B PRO C 854 197.5 133.8 47.5 33 B PRO O 854 198.5 133.4 46.9 34 B GLY N 855 197.0 135.0 47.3 34 B GLY CA 855 197.7 135.9 46.4 35 B GLY C 855 196.9 136.1 45.2 36 B GLY O 855 196.9 137.2 44.6 37 B LYS N 856 196.1 135.1 44.8 36 B LYS CA 856 195.3 135.1 43.7 35 B LYS CB 856 195.1 133.6 43.2 35 B LYS CG 856 196.4 133.0 42.7 35 B LYS CD 856 197.1 134.0 41.8 35 B LYS CE 856 198.4 133.4 41.2 36 B LYS NZ 856 198.2 132.4 40.1 36 B LYS C 856 193.9 135.7 44.0 35 B LYS O 856 193.5 135.7 45.1 35 B SER N 857 193.3 136.2 42.9 36 B SER CA 857 192.0 136.8 43.0 36 B SER CB 857 191.8 137.8 41.9 36 B SER OG 857 191.6 139.1 42.3 37 B SER C 857 190.8 135.9 43.1 36 B SER O 857 190.9 134.7 42.7 38 B ARG N 858 189.6 136.4 43.5 35 B ARG CA 858 188.4 135.6 43.7 34 B ARG CB 858 187.6 136.1 44.8 34 B ARG CG 858 186.8 137.3 44.6 34 B ARG CD 858 186.4 138.1 45.8 34 B ARG NE 858 185.4 139.1 45.5 34 B ARG CZ 858 184.5 139.6 46.4 33 B ARG NH1 858 184.5 139.2 47.7 33 B ARG NH2 858 183.6 140.5 46.0 33 B ARG C 858 187.6 135.7 42.4 33 B ARG O 858 187.8 136.6 41.6 33 B ASP N 859 186.8 134.7 42.1 32 B ASP CA 859 185.9 134.6 41.0 31 B ASP CB 859 186.6 134.6 39.6 32 B ASP CG 859 187.6 133.4 39.5 33 B ASP OD1 859 187.2 132.3 39.3 33 B ASP OD2 859 188.8 133.7 39.6 34 B ASP C 859 185.0 133.5 41.2 31 B ASP O 859 185.2 132.6 42.0 30 B PHE N 860 183.9 133.5 40.4 30 B PHE CA 860 182.8 132.4 40.5 30 B PHE CB 860 181.6 132.9 39.7 29 B PHE CG 860 181.2 134.3 40.2 30 B PHE CD1 860 181.5 135.4 39.4 30 B PHE CD2 860 180.4 134.4 41.4 30 B PHE CE1 860 181.1 136.7 39.9 30 B PHE CE2 860 180.1 135.7 41.8 30 B PHE CZ 860 180.5 136.8 41.1 30 B PHE C 860 183.3 131.0 40.2 29 B PHE O 860 182.8 130.1 40.8 30 B TYR N 861 184.2 130.9 39.2 28 B TYR CA 861 184.7 129.6 38.8 25 B TYR CB 861 185.6 129.8 37.5 21 B TYR CG 861 186.5 128.6 37.2 17 B TYR CD1 861 186.0 127.4 36.8 16 B TYR CE1 861 186.8 126.2 36.6 13 B TYR CD2 861 187.9 128.6 37.5 15 B TYR CE2 861 188.7 127.5 37.4 13 B TYR CZ 861 188.1 126.3 36.9 12 B TYR OH 861 188.9 125.2 36.9  9 B TYR C 861 185.4 128.9 40.0 25 B TYR O 861 185.3 127.7 40.2 25 B HIS N 862 186.2 129.7 40.7 25 B HIS CA 862 186.9 129.0 41.9 26 B HIS CB 862 188.1 129.8 42.3 26 B HIS CG 862 189.2 129.9 41.3 26 B HIS CD2 862 190.2 129.0 41.1 27 B HIS ND1 862 189.2 130.8 40.3 27 B HIS CE1 862 190.2 130.6 39.5 28 B HIS NE2 862 190.9 129.5 40.0 28 B HIS C 862 186.0 128.9 43.0 27 B HIS O 862 186.2 128.0 43.9 26 B THR N 863 185.0 129.8 43.2 28 B THR CA 863 184.0 129.7 44.2 30 B THR CB 863 182.9 130.8 44.1 31 B THR OG1 863 183.5 132.1 44.1 32 B THR CG2 863 181.8 130.6 45.2 30 B THR C 863 183.3 128.3 44.0 31 B THR O 863 183.4 127.4 44.9 32 B CYS N 864 182.8 128.2 42.8 30 B CYS CA 864 182.1 127.0 42.4 28 B CYS CB 864 181.7 127.1 41.0 29 B CYS SG 864 181.2 125.5 40.4 30 B CYS C 864 183.0 125.7 42.6 27 B CYS O 864 182.5 124.8 43.2 28 B TYR N 865 184.2 125.8 42.1 26 B TYR CA 865 185.0 124.6 42.2 25 B TYR CB 865 185.9 124.4 41.0 25 B TYR CG 865 185.2 124.1 39.7 24 B TYR CD1 865 184.6 125.1 38.9 24 B TYR CE1 865 183.8 124.8 37.9 25 B TYR CD2 865 184.8 122.8 39.5 24 B TYR CE2 865 184.0 122.5 38.4 25 B TYR CZ 865 183.4 123.5 37.6 25 B TYR OH 865 182.5 123.2 36.6 27 B TYR C 865 185.6 124.3 43.5 24 B TYR O 865 185.7 123.1 43.9 25 B CYS N 866 185.9 125.3 44.3 24 B CYS CA 866 186.5 125.0 45.7 23 B CYS CB 866 187.1 126.3 46.3 22 B CYS SG 866 188.6 126.8 45.6 23 B CYS C 866 185.4 124.5 46.6 23 B CYS O 866 185.7 123.6 47.4 22 B LEU N 867 184.2 124.9 46.4 23 B LEU CA 867 183.1 124.4 47.2 24 B LEU CB 867 181.9 125.4 47.1 22 B LEU CG 867 182.2 126.8 47.7 22 B LEU CD1 867 180.9 127.6 47.4 22 B LEU CD2 867 182.5 126.7 49.2 21 B LEU C 867 182.8 123.0 46.7 26 B LEU O 867 182.7 122.1 47.5 26 B SER N 868 182.6 122.9 45.4 27 B SER CA 868 182.4 121.6 44.8 28 B SER CB 868 182.4 121.6 43.3 27 B SER OG 868 181.3 122.4 42.7 26 B SER C 868 183.4 120.5 45.4 29 B SER O 868 183.1 119.4 45.9 29 B GLY N 869 184.7 120.9 45.3 30 B GLY CA 869 185.8 120.1 45.8 31 B GLY C 869 185.8 119.9 47.3 32 B GLY O 869 186.3 118.9 47.8 32 B LEU N 870 185.2 120.8 48.0 33 B LEU CA 870 185.1 120.7 49.5 33 B LEU CB 870 184.7 122.0 50.1 32 B LEU CG 870 184.6 122.2 51.6 30 B LEU CD1 870 186.0 121.8 52.2 29 B LEU CD2 870 184.2 123.6 52.0 28 B LEU C 870 184.1 119.6 49.9 34 B LEU O 870 184.3 118.7 50.6 34 B SER N 871 182.9 119.8 49.2 35 B SER CA 871 181.8 118.9 49.4 36 B SER CB 871 180.7 119.2 48.3 36 B SER OG 871 179.5 118.6 48.6 37 B SER C 871 182.2 117.4 49.1 36 B SER O 871 181.9 116.6 50.0 37 B ILE N 872 182.9 117.2 48.1 36 B ILE CA 872 183.4 115.8 47.8 36 B ILE CB 872 184.1 115.8 46.4 34 B ILE CG2 872 185.2 114.7 46.3 34 B ILE CG1 872 183.0 115.4 45.3 33 B ILE CD1 872 183.4 115.9 44.0 32 B ILE C 872 184.3 115.3 48.9 36 B ILE O 872 184.1 114.3 49.5 36 B ALA N 873 185.3 116.1 49.3 36 B ALA CA 873 186.2 115.7 50.3 38 B ALA CB 873 187.3 116.8 50.5 38 B ALA C 873 185.6 115.4 51.7 38 B ALA O 873 186.2 114.8 52.5 38 B GLN N 874 184.4 115.9 51.9 38 B GLN CA 874 183.7 115.7 53.1 39 B GLN CB 874 183.3 117.1 53.7 38 B GLN CG 874 182.4 117.9 52.9 36 B GLN CD 874 182.0 119.2 53.6 36 B GLN OE1 874 180.9 119.8 53.3 35 B GLN NE2 874 182.8 119.7 54.6 34 B GLN C 874 182.5 114.8 53.1 41 B GLN O 874 181.9 114.5 54.1 41 B HIS N 875 182.2 114.2 51.9 43 B HIS CA 875 181.1 113.3 51.8 45 B HIS CB 875 180.0 113.9 51.0 44 B HIS CG 875 179.3 115.1 51.6 45 B HIS CD2 875 178.3 115.9 51.2 45 B HIS ND1 875 179.5 115.4 52.9 45 B HIS CE1 875 178.8 116.5 53.3 45 B HIS NE2 875 178.0 116.8 52.2 45 B HIS C 875 181.5 112.0 51.1 47 B HIS O 875 182.0 112.0 49.9 47 B PHE N 876 181.5 110.9 51.8 50 B PHE CA 876 181.8 109.6 51.3 52 B PHE CB 876 182.9 108.9 52.2 51 B PHE CG 876 183.1 107.5 51.7 50 B PHE CD1 876 184.1 107.2 50.8 50 B PHE CD2 876 182.3 106.5 52.1 50 B PHE CE1 876 184.3 106.0 50.3 50 B PHE CE2 876 182.4 105.2 51.6 50 B PHE CZ 876 183.5 104.9 50.7 50 B PHE C 876 180.6 108.7 51.2 54 B PHE O 876 179.6 108.8 52.0 54 B GLY N 877 180.6 107.8 50.2 57 B GLY CA 877 179.5 106.9 50.0 61 B GLY C 877 179.9 105.7 49.2 64 B GLY O 877 180.6 105.8 48.2 65 B SER N 878 179.4 104.5 49.6 65 B SER CA 878 179.7 103.3 48.9 67 B SER CB 878 181.0 102.7 49.4 67 B SER OG 878 181.8 102.0 48.4 67 B SER C 878 178.5 102.4 49.1 68 B SER O 878 178.6 101.4 49.8 68 B GLY N 879 177.4 102.7 48.4 68 B GLY CA 879 176.2 101.9 48.5 69 B GLY C 879 175.5 102.3 49.8 69 B GLY O 879 175.1 103.5 49.9 69 B ALA N 880 175.4 101.4 50.7 69 B ALA CA 880 174.8 101.7 52.0 69 B ALA CB 880 174.4 100.3 52.7 69 B ALA C 880 175.7 102.5 52.9 69 B ALA O 880 175.4 103.0 54.0 69 B MET N 881 177.0 102.5 52.5 68 B MET CA 881 178.0 103.3 53.2 67 B MET CB 881 179.4 102.8 52.7 67 B MET CG 881 180.0 101.7 53.5 68 B MET SD 881 178.9 100.3 53.6 69 B MET CE 881 178.3 100.6 55.3 69 B MET C 881 177.9 104.8 52.9 65 B MET O 881 177.6 105.2 51.8 65 B LEU N 882 178.2 105.5 54.0 64 B LEU CA 882 178.1 107.0 54.0 62 B LEU CB 882 176.7 107.5 54.1 62 B LEU CG 882 175.7 107.6 53.0 63 B LEU CD1 882 176.4 108.2 51.7 63 B LEU CD2 882 175.1 106.3 52.6 63 B LEU C 882 179.0 107.5 55.1 60 B LEU O 882 178.6 107.4 56.3 61 B HIS N 883 180.1 108.1 54.8 59 B HIS CA 883 180.9 108.6 55.9 58 B HIS CB 883 182.2 107.8 56.2 57 B HIS CG 883 183.0 108.3 57.3 58 B HIS CD2 883 183.8 109.4 57.4 58 B HIS ND1 883 183.3 107.5 58.4 58 B HIS CE1 883 184.0 108.2 59.3 59 B HIS NE2 883 184.4 109.3 58.7 58 B HIS C 883 181.3 110.1 55.6 57 B HIS O 883 181.9 110.4 54.6 57 B ASP N 884 181.0 111.0 56.5 54 B ASP CA 884 181.3 112.4 56.4 52 B ASP CB 884 180.1 113.3 56.8 52 B ASP CG 884 179.0 113.2 55.8 52 B ASP OD1 884 178.1 114.1 55.9 52 B ASP OD2 884 179.0 112.4 54.9 52 B ASP C 884 182.5 112.8 57.2 51 B ASP O 884 182.8 112.1 58.2 51 B VAL N 885 183.2 113.8 56.8 50 B VAL CA 885 184.3 114.4 57.5 49 B VAL CB 885 185.7 113.9 57.0 48 B VAL CG1 885 186.8 114.6 57.7 47 B VAL CG2 885 185.9 112.4 57.2 48 B VAL C 885 184.2 115.9 57.3 49 B VAL O 885 184.4 116.4 56.2 49 B VAL N 886 183.8 116.6 58.3 48 B VAL CA 886 183.7 118.1 58.2 49 B VAL CB 886 182.4 118.6 58.6 49 B VAL CG1 886 182.4 120.1 58.4 49 B VAL CG2 886 181.3 118.0 57.7 49 B VAL C 886 184.8 118.7 59.0 50 B VAL O 886 185.0 118.2 60.2 51 B MET N 887 185.6 119.5 58.5 51 B MET CA 887 186.7 120.2 59.2 51 B MET CB 887 187.9 120.4 58.3 51 B MET CG 887 188.6 119.2 57.9 50 B MET SD 887 188.9 118.2 59.4 50 B MET CE 887 190.4 118.9 59.9 49 B MET C 887 186.2 121.5 59.8 53 B MET O 887 185.5 122.2 59.2 52 B GLY N 888 186.7 121.7 61.1 54 B GLY CA 888 186.3 122.9 61.8 55 B GLY C 888 184.8 122.9 62.2 55 B GLY O 888 184.2 121.9 62.5 55 B VAL N 889 184.3 124.1 62.3 55 B VAL CA 889 182.9 124.2 62.8 56 B VAL CB 889 182.5 125.7 62.9 57 B VAL CG1 889 181.6 126.1 61.7 57 B VAL CG2 889 181.9 125.9 64.2 58 B VAL C 889 182.0 123.3 61.9 55 B VAL O 889 182.0 123.4 60.7 55 B PRO N 890 181.1 122.5 62.5 55 B PRO CD 890 181.0 122.3 64.0 55 B PRO CA 890 180.2 121.6 61.8 55 B PRO CB 890 179.4 121.0 63.0 55 B PRO CG 890 179.6 122.0 64.1 55 B PRO C 890 179.3 122.3 60.8 54 B PRO O 890 178.7 121.6 59.9 54 B GLU N 891 179.2 123.6 60.9 54 B GLU CA 891 178.3 124.3 59.9 54 B GLU CB 891 178.1 125.8 60.4 55 B GLU CG 891 177.1 126.0 61.6 56 B GLU CD 891 177.6 125.4 62.9 58 B GLU OE1 891 178.8 125.3 63.1 58 B GLU OE2 891 176.7 124.9 63.7 58 B GLU C 891 179.1 124.3 58.6 54 B GLU O 891 178.5 124.7 57.5 53 B ASN N 892 180.3 123.9 58.6 53 B ASN CA 892 181.1 123.8 57.4 51 B ASN CB 892 182.6 123.7 57.7 49 B ASN CG 892 183.2 124.9 58.5 48 B ASN OD1 892 184.2 124.8 59.1 47 B ASN ND2 892 182.5 126.0 58.5 47 B ASN C 892 180.7 122.6 56.5 51 B ASN O 892 181.5 122.1 55.7 53 B VAL N 893 179.5 122.1 56.7 50 B VAL CA 893 179.1 121.0 55.8 49 B VAL CB 893 178.4 119.9 56.6 49 B VAL CG1 893 177.1 120.4 57.3 50 B VAL CG2 893 178.0 118.7 55.7 49 B VAL C 893 178.2 121.5 54.7 48 B VAL O 893 177.1 122.1 55.0 49 B LEU N 894 178.6 121.2 53.5 47 B LEU CA 894 177.9 121.6 52.3 46 B LEU CB 894 178.9 122.0 51.2 46 B LEU CG 894 180.1 122.8 51.4 46 B LEU CD1 894 181.0 122.8 50.2 46 B LEU CD2 894 179.8 124.2 51.8 47 B LEU C 894 177.0 120.5 51.8 45 B LEU O 894 177.2 119.3 52.1 45 B GLN N 895 176.0 120.9 51.0 44 B GLN CA 895 175.1 119.9 50.3 44 B GLN CB 895 174.1 120.6 49.5 44 B GLN CG 895 173.0 121.3 50.3 46 B GLN CD 895 172.2 120.3 51.1 46 B GLN OE1 895 171.4 119.6 50.5 46 B GLN NE2 895 172.5 120.3 52.4 47 B GLN C 895 176.0 119.1 49.4 44 B GLN O 895 177.0 119.5 48.9 44 B PRO N 896 175.7 117.8 49.3 43 B PRO CD 896 174.7 117.0 50.0 43 B PRO CA 896 176.5 116.9 48.4 42 B PRO CB 896 176.0 115.5 48.8 42 B PRO CG 896 174.6 115.8 49.2 42 B PRO C 896 176.3 117.2 46.9 41 B PRO O 896 175.2 117.6 46.5 41 B THR N 897 177.3 116.9 46.1 39 B THR CA 897 177.3 117.1 44.7 37 B THR CB 897 178.4 118.2 44.2 38 B THR OG1 897 178.2 118.5 42.8 38 B THR CG2 897 179.8 117.9 44.5 37 B THR C 897 177.6 115.8 44.0 35 B THR O 897 178.4 114.9 44.5 35 B HIS N 898 177.0 115.5 42.9 33 B HIS CA 898 177.1 114.3 42.1 31 B HIS CB 898 176.0 114.2 41.1 32 B HIS CG 898 175.9 112.9 40.4 33 B HIS CD2 898 174.8 112.2 40.0 33 B HIS ND1 898 177.0 112.2 40.0 33 B HIS CE1 898 176.6 111.1 39.3 33 B HIS NE2 898 175.2 111.1 39.3 33 B HIS C 898 178.5 114.4 41.3 31 B HIS O 898 178.6 115.2 40.5 31 B PRO N 899 179.4 113.5 41.6 29 B PRO CD 899 179.4 112.5 42.7 29 B PRO CA 899 180.7 113.5 41.0 28 B PRO CB 899 181.5 112.4 41.7 28 B PRO CG 899 180.4 111.5 42.2 30 B PRO C 899 180.9 113.3 39.4 27 B PRO O 899 182.0 113.4 38.9 27 B VAL N 900 179.8 113.1 38.7 25 B VAL CA 900 179.9 113.0 37.3 23 B VAL CB 900 179.1 111.9 36.6 22 B VAL CG1 900 179.0 112.1 35.1 21 B VAL CG2 900 179.7 110.5 36.9 21 B VAL C 900 179.5 114.3 36.7 24 B VAL O 900 180.3 115.0 36.0 24 B TYR N 901 178.3 114.8 37.1 25 B TYR CA 901 177.7 116.0 36.7 25 B TYR CB 901 176.2 115.9 36.6 23 B TYR CG 901 175.8 114.8 35.7 23 B TYR CD1 901 175.5 113.5 36.3 24 B TYR CE1 901 175.1 112.4 35.5 24 B TYR CD2 901 175.6 114.9 34.4 23 B TYR CE2 901 175.2 113.9 33.6 24 B TYR CZ 901 174.9 112.6 34.1 24 B TYR OH 901 174.6 111.6 33.3 24 B TYR C 901 178.0 117.3 37.5 26 B TYR O 901 177.8 118.4 37.1 26 B ASN N 902 178.5 117.0 38.7 26 B ASN CA 902 178.8 118.1 39.7 26 B ASN CB 902 180.0 118.9 39.3 26 B ASN CG 902 180.5 119.8 40.3 26 B ASN OD1 902 180.6 119.4 41.5 25 B ASN ND2 902 180.7 121.1 40.0 26 B ASN C 902 177.6 119.0 40.0 27 B ASN O 902 177.7 120.2 39.8 27 B ILE N 903 176.5 118.4 40.3 28 B ILE CA 903 175.3 119.1 40.7 28 B ILE CB 903 174.3 119.3 39.5 27 B ILE CG2 903 175.1 119.9 38.3 27 B ILE CG1 903 173.6 118.1 39.0 26 B ILE CD1 903 172.6 118.3 37.9 24 B ILE C 903 174.6 118.1 41.7 31 B ILE O 903 175.0 117.0 41.7 32 B GLY N 904 173.7 118.6 42.5 34 B GLY CA 904 173.1 117.8 43.5 35 B GLY C 904 172.6 116.5 43.0 36 B GLY O 904 171.8 116.5 41.9 36 B PRO N 905 172.9 115.4 43.6 36 B PRO CD 905 173.6 115.4 44.9 36 B PRO CA 905 172.5 114.0 43.3 37 B PRO CB 905 172.7 113.2 44.5 36 B PRO CG 905 173.9 113.9 45.1 36 B PRO C 905 171.0 114.0 42.9 38 B PRO O 905 170.6 113.3 41.9 38 B ASP N 906 170.2 114.7 43.7 41 B ASP CA 906 168.8 114.8 43.5 44 B ASP CB 906 168.2 115.5 44.7 46 B ASP CG 906 169.0 116.6 45.2 48 B ASP OD1 906 169.9 116.4 46.1 50 B ASP OD2 906 168.9 117.7 44.6 50 B ASP C 906 168.4 115.5 42.2 43 B ASP O 906 167.3 115.2 41.7 44 B LYS N 907 169.2 116.4 41.8 43 B LYS CA 907 168.9 117.1 40.5 43 B LYS CB 907 169.8 118.4 40.4 43 B LYS CG 907 169.6 119.4 41.5 42 B LYS CD 907 168.2 119.8 41.6 43 B LYS CE 907 167.9 120.7 42.7 43 B LYS NZ 907 166.5 121.3 42.7 44 B LYS C 907 169.2 116.2 39.4 42 B LYS O 907 168.4 116.1 38.5 42 B VAL N 908 170.3 115.4 39.6 42 B VAL CA 908 170.7 114.4 38.6 42 B VAL CB 908 172.0 113.7 39.0 41 B VAL CG1 908 172.4 112.7 37.9 41 B VAL CG2 908 173.1 114.7 39.2 41 B VAL C 908 169.6 113.4 38.4 42 B VAL O 908 169.1 113.1 37.3 42 B ILE N 909 169.0 113.0 39.6 42 B ILE CA 909 168.0 112.0 39.6 42 B ILE CB 909 167.7 111.5 41.1 43 B ILE CG2 909 166.4 110.7 41.1 43 B ILE CG1 909 168.9 110.7 41.6 42 B ILE CD1 909 168.9 110.4 43.0 43 B ILE C 909 166.7 112.6 39.1 42 B ILE O 909 166.1 112.1 38.1 42 B GLN N 910 166.3 113.8 39.6 42 B GLN CA 910 165.1 114.5 39.2 42 B GLN CB 910 165.2 115.9 39.8 44 B GLN CG 910 163.9 116.7 39.8 46 B GLN CD 910 163.9 117.8 40.8 47 B GLN OE1 910 163.1 118.7 40.7 48 B GLN NE2 910 164.7 117.7 41.9 48 B GLN C 910 165.1 114.7 37.6 42 B GLN O 910 164.2 114.3 36.9 42 B ALA N 911 166.1 115.3 37.1 41 B ALA CA 911 166.2 115.6 35.7 40 B ALA CB 911 167.4 116.4 35.3 40 B ALA C 911 166.1 114.4 34.8 39 B ALA O 911 165.4 114.4 33.8 39 B THR N 912 166.9 113.3 35.1 40 B THR CA 912 166.9 112.1 34.3 40 B THR CB 912 168.0 111.1 34.8 40 B THR OG1 912 167.7 110.7 36.2 41 B THR CG2 912 169.4 111.6 34.7 40 B THR C 912 165.6 111.4 34.2 41 B THR O 912 165.2 111.1 33.1 41 B THR N 913 164.9 111.2 35.3 41 B THR CA 913 163.6 110.5 35.3 40 B THR CB 913 163.1 110.1 36.7 40 B THR OG1 913 162.0 110.9 37.1 40 B THR CG2 913 164.1 110.1 37.8 39 B THR C 913 162.6 111.4 34.5 40 B THR O 913 161.8 110.8 33.8 41 B HIS N 914 162.6 112.7 34.8 40 B HIS CA 914 161.7 113.5 34.1 39 B HIS CB 914 161.8 115.0 34.6 38 B HIS CG 914 161.1 115.9 33.7 38 B HIS CD2 914 159.8 116.4 33.7 38 B HIS ND1 914 161.6 116.3 32.5 37 B HIS CE1 914 160.7 117.0 31.8 37 B HIS NE2 914 159.6 117.1 32.5 39 B HIS C 914 161.9 113.5 32.6 39 B HIS O 914 160.9 113.4 31.8 39 B PHE N 915 163.1 113.6 32.1 40 B PHE CA 915 163.4 113.6 30.7 40 B PHE CB 915 164.8 114.1 30.4 38 B PHE CG 915 165.0 115.6 30.4 36 B PHE CD1 915 165.5 116.2 31.6 36 B PHE CD2 915 164.4 116.4 29.4 35 B PHE CE1 915 165.6 117.6 31.7 35 B PHE CE2 915 164.5 117.8 29.5 35 B PHE CZ 915 165.1 118.4 30.6 35 B PHE C 915 163.2 112.2 30.1 41 B PHE O 915 162.9 112.0 28.9 40 B LEU N 916 163.2 111.2 31.0 42 B LEU CA 916 162.9 109.8 30.7 44 B LEU CB 916 163.2 108.9 31.9 44 B LEU CG 916 164.4 107.9 31.8 45 B LEU CD1 916 165.4 108.4 30.8 45 B LEU CD2 916 165.1 107.8 33.2 45 B LEU C 916 161.5 109.7 30.2 45 B LEU O 916 161.2 108.9 29.3 45 B GLN N 917 160.6 110.5 30.8 47 B GLN CA 917 159.2 110.5 30.4 49 B GLN CB 917 158.4 111.6 31.0 50 B GLN CG 917 158.6 111.8 32.5 52 B GLN CD 917 158.0 113.1 33.0 54 B GLN OE1 917 158.5 113.8 33.8 55 B GLN NE2 917 156.8 113.4 32.4 54 B GLN C 917 159.1 110.8 28.9 49 B GLN O 917 158.0 110.7 28.3 49 B LYS N 918 160.2 111.3 28.3 51 B LYS CA 918 160.2 111.6 26.9 53 B LYS CB 918 160.7 113.0 26.6 54 B LYS CG 918 159.9 114.1 27.4 55 B LYS CD 918 160.5 114.3 28.8 55 B LYS CE 918 159.5 115.2 29.6 56 B LYS NZ 918 159.2 116.5 29.0 56 B LYS C 918 161.0 110.6 26.1 54 B LYS O 918 161.9 110.0 26.6 53 B PRO N 919 160.7 110.4 24.8 55 B PRO CD 919 159.5 110.9 24.1 55 B PRO CA 919 161.4 109.4 24.0 56 B PRO CB 919 160.4 109.1 22.9 56 B PRO CG 919 159.7 110.5 22.7 55 B PRO C 919 162.6 110.1 23.4 58 B PRO O 919 162.7 111.3 23.2 59 B VAL N 920 163.7 109.3 23.2 60 B VAL CA 920 164.9 109.8 22.6 61 B VAL CB 920 165.9 108.7 22.4 61 B VAL CG1 920 167.1 109.1 21.5 61 B VAL CG2 920 166.4 108.1 23.7 61 B VAL C 920 164.4 110.3 21.2 64 B VAL O 920 163.7 109.5 20.6 64 B PRO N 921 164.7 111.5 20.8 66 B PRO CD 921 165.4 112.6 21.6 66 B PRO CA 921 164.3 112.0 19.5 68 B PRO CB 921 165.1 113.3 19.3 67 B PRO CG 921 165.1 113.8 20.7 66 B PRO C 921 164.5 111.0 18.4 72 B PRO O 921 165.6 110.8 17.9 72 B GLY N 922 163.5 110.2 18.1 75 B GLY CA 922 163.5 109.2 17.1 80 B GLY C 922 163.6 109.6 15.6 83 B GLY O 922 163.5 110.8 15.3 84 B PHE N 923 163.7 108.6 14.8 87 B PHE CA 923 163.7 108.8 13.3 90 B PHE CB 923 165.2 108.7 12.8 91 B PHE CG 923 166.2 109.2 13.8 93 B PHE CD1 923 166.7 110.5 13.8 93 B PHE CD2 923 166.8 108.3 14.8 93 B PHE CE1 923 167.6 111.0 14.8 93 B PHE CE2 923 167.7 108.7 15.7 93 B PHE CZ 923 168.1 110.1 15.7 93 B PHE C 923 162.9 107.7 12.7 91 B PHE OT1 923 163.4 106.5 12.5 91 B PHE OT2 923 161.7 107.9 12.6 92 B ZIN ZN 1000 192.2 127.2 39.0 29 Z FPP P 2001 197.5 126.4 33.3 35 F FPP O 2001 197.4 128.0 33.4 36 F FPP O1 2001 199.0 126.1 32.7 36 F FPP O2 2001 197.2 125.9 34.8 37 F FPP O3 2001 196.4 125.9 32.3 34 F FPP C 2001 196.2 124.5 31.9 32 F FPP C1 2001 194.1 123.9 30.6 29 F FPP C2 2001 194.8 124.1 31.7 30 F FPP C3 2001 192.6 123.6 30.6 27 F FPP C4 2001 194.7 124.0 29.2 29 F FPP C5 2001 192.2 122.5 31.7 26 F FPP C6 2001 189.8 122.3 32.6 22 F FPP C7 2001 190.7 122.1 31.6 24 F FPP C8 2001 189.9 123.4 33.6 22 F FPP C9 2001 188.5 121.5 32.6 21 F FPP C10 2001 187.4 122.1 31.8 20 F FPP C11 2001 186.1 121.4 31.9 20 F FPP C12 2001 184.9 121.6 31.2 20 F FPP C13 2001 184.8 122.8 30.3 20 F FPP C14 2001 183.7 120.7 31.2 20 F FPP P1 2001 198.0 124.6 35.3 37 F FPP O4 2001 197.4 124.2 36.8 37 F FPP O5 2001 197.7 123.3 34.3 36 F FPP O6 2001 199.6 124.9 35.5 37 F SCH C1 2002 187.7 127.3 33.2 31 I SCH C2 2002 187.2 128.3 32.5 31 I SCH C3 2002 188.0 129.4 32.1 31 I SCH C4 2002 189.1 129.2 31.1 32 I SCH C5 2002 190.1 128.2 31.3 32 I SCH C6 2002 190.2 127.2 32.5 32 I SCH C7 2002 189.2 127.4 33.7 31 I SCH C8 2002 185.9 128.2 32.1 31 I SCH C9 2002 187.0 126.2 33.6 30 I SCH C10 2002 185.6 126.1 33.2 30 I SCH C11 2002 185.1 127.2 32.4 30 I SCH N12 2002 189.2 130.0 30.0 32 I SCH C13 2002 190.1 129.9 29.1 33 I SCH C14 2002 191.2 128.9 29.2 33 I SCH C15 2002 191.1 128.1 30.4 33 I SCH C16 2002 187.8 130.6 32.7 33 I SCH C17 2002 188.7 131.8 32.5 34 I SCH C18 2002 189.1 132.5 33.8 34 I SCH N19 2002 188.0 132.6 34.7 35 I SCH C20 2002 187.4 131.3 35.0 35 I SCH C21 2002 186.7 130.7 33.8 34 I SCH BR22 2002 192.6 128.7 28.0 32 I SCH CL23 2002 184.6 124.8 33.5 30 I SCH BR24 2002 185.1 129.6 31.1 34 I SCH C25 2002 187.5 133.7 35.3 35 I SCH O26 2002 186.6 133.8 36.1 36 I SCH C27 2002 188.3 134.9 34.8 35 I SCH C28 2002 188.0 136.1 35.7 35 I SCH C29 2002 187.2 137.1 35.2 35 I SCH C30 2002 187.0 138.3 36.0 36 I SCH N31 2002 187.5 138.4 37.2 37 I SCH C32 2002 188.3 137.4 37.8 36 I SCH C33 2002 188.5 136.2 37.0 36 I SCH O34 2002 187.3 139.5 38.0 39 I HOH OH2 1002 188.6 130.2 17.2 10 W HOH OH2 1003 202.5 124.5 44.4  7 W HOH OH2 1004 204.1 118.0 25.8 20 W HOH OH2 1005 199.0 115.7 20.4 15 W HOH OH2 1007 200.6 115.3 35.1 19 W HOH OH2 1009 192.7 123.7 17.5 21 W HOH OH2 1011 197.7 118.0 19.2  4 W HOH OH2 1012 205.7 120.4 35.2 14 W HOH OH2 1016 203.8 109.9 23.4 33 W HOH OH2 1019 195.2 119.4 18.6 26 W HOH OH2 1020 180.3 133.7 21.4 15 W HOH OH2 1021 204.3 120.9 32.8 17 W HOH OH2 1022 208.0 126.4 33.6 22 W HOH OH2 1023 205.0 127.9 36.8 27 W HOH OH2 1024 182.3 104.6 22.8 39 W HOH OH2 1026 178.5 138.5 19.7 13 W HOH OH2 1032 205.9 125.5 36.7 19 W HOH OH2 1033 198.8 103.8 28.4 20 W HOH OH2 1034 204.1 120.1 48.4 30 W HOH OH2 1038 191.1 121.4 16.9 36 W HOH OH2 1039 210.6 125.7 33.2 19 W HOH OH2 1042 193.4 121.9 45.3 19 W HOH OH2 1044 194.7 140.1 8.3 21 W HOH OH2 1045 192.7 118.9 18.4 44 W HOH OH2 1046 202.5 115.9 46.7 43 W HOH OH2 1050 180.6 128.1 15.7 40 W HOH OH2 1051 190.8 139.7 25.1 28 W HOH OH2 1052 207.2 134.0 14.1 23 W HOH OH2 1054 191.7 116.7 17.3 34 W HOH OH2 1055 194.9 139.9 5.6 15 W HOH OH2 1061 176.7 138.2 26.5 29 W HOH OH2 1063 203.4 139.4 14.3 31 W HOH OH2 1064 196.2 113.7 18.7 43 W HOH OH2 1065 208.1 125.0 11.6 23 W HOH OH2 1066 179.4 139.4 43.7 51 W HOH OH2 1067 186.2 130.2 16.2 31 W HOH OH2 1068 186.8 126.4 10.1 29 W HOH OH2 1070 186.0 115.0 21.9 53 W HOH OH2 1071 207.5 109.0 11.3 19 W HOH OH2 1073 202.2 111.5 25.7 23 W HOH OH2 1074 201.6 108.0 25.8 30 W HOH OH2 1075 212.3 127.0 31.7 25 W HOH OH2 1076 208.1 134.9 17.1 28 W HOH OH2 1077 204.6 113.1 35.4 16 W HOH OH2 1078 208.3 128.4 31.9 30 W HOH OH2 1080 188.2 112.1 12.4 51 W HOH OH2 1081 204.2 111.6 11.5 19 W HOH OH2 1082 178.8 126.3 16.7 41 W HOH OH2 1084 175.5 122.9 14.3 25 W HOH OH2 1085 204.2 128.2 9.1 24 W HOH OH2 1087 208.8 137.6 21.9 35 W HOH OH2 1089 212.3 130.1 29.5 35 W HOH OH2 1090 180.0 103.2 35.0 49 W HOH OH2 1091 185.5 128.6 11.0 31 W HOH OH2 1092 212.9 126.4 29.3 30 W HOH OH2 1093 202.1 109.9 39.4 39 W HOH OH2 1095 199.7 109.4 24.5 35 W HOH OH2 1096 188.4 124.2 11.5 34 W HOH OH2 1097 190.7 103.3 22.8 33 W HOH OH2 1098 185.6 159.1 8.2 35 W HOH OH2 1099 187.1 128.1 18.4 37 W HOH OH2 1100 188.0 125.1 8.0 39 W HOH OH2 1102 201.5 137.5 27.9 51 W HOH OH2 1103 193.1 142.2 18.2 45 W HOH OH2 1104 214.0 114.3 16.4 13 W HOH OH2 1105 204.5 118.2 41.3 16 W HOH OH2 1106 188.4 106.6 46.3 36 W HOH OH2 1107 179.7 115.9 47.9 42 W HOH OH2 1109 189.2 100.9 23.9 47 W HOH OH2 1110 205.0 130.9 42.4 25 W HOH OH2 1111 212.1 123.9 29.9 30 W HOH OH2 1112 177.1 128.5 13.5 19 W HOH OH2 1113 201.0 107.3 44.3 27 W HOH OH2 1114 187.4  99.1 21.7 34 W HOH OH2 1115 198.8 142.7 13.6 46 W HOH OH2 1116 175.1 118.7 31.2 26 W HOH OH2 1117 221.5 119.8 25.3 32 W HOH OH2 1118 209.4 133.2 48.8 26 W HOH OH2 1119 175.9 108.0 36.0 30 W HOH OH2 1120 183.3 100.4 23.5 44 W HOH OH2 1121 201.6 133.0 32.9 62 W HOH OH2 1122 197.8 114.8 15.0 38 W HOH OH2 1123 211.3 128.0 27.8 25 W HOH OH2 1124 163.2 134.5 25.1 33 W HOH OH2 1125 214.5 128.0 21.9 39 W HOH OH2 1126 221.0 126.1 31.6 48 W HOH OH2 1127 199.4 103.8 31.4 31 W HOH OH2 1128 211.3 135.8 24.5 38 W HOH OH2 1129 201.5 109.0 21.8 42 W HOH OH2 1130 173.1 144.3 28.1 30 W HOH OH2 1131 196.0 111.8 47.6 18 W HOH OH2 1132 202.6 109.7 13.2 55 W HOH OH2 1133 215.3 130.2 29.7 37 W HOH OH2 1134 212.4 124.6 17.2 28 W HOH OH2 1135 189.5 114.6 16.1 40 W HOH OH2 1136 169.0 123.2 22.2 43 W HOH OH2 1137 178.4 141.1 24.5 23 W HOH OH2 1138 219.5 124.8 26.0 40 W HOH OH2 1139 195.1 142.1 3.9 40 W HOH OH2 1140 211.5 120.1 16.1 22 W HOH OH2 1141 182.3 139.1 23.7 36 W HOH OH2 1142 178.3 112.2 46.7 50 W HOH OH2 1143 186.5 152.1 10.2 32 W HOH OH2 1144 173.1 139.5 17.8 40 W HOH OH2 1145 215.5 102.4 15.6 39 W HOH OH2 1146 214.8 107.2 19.7 35 W HOH OH2 1147 219.5 123.5 49.3 46 W HOH OH2 1148 201.0  97.3 26.4 49 W HOH OH2 1149 211.5 134.0 17.1 43 W HOH OH2 1150 204.4 135.8 11.3 36 W HOH OH2 1151 178.7 141.7 41.7 23 W HOH OH2 1152 221.6 124.6 40.7 59 W HOH OH2 1155 196.1 124.1 18.2 20 W HOH OH2 1156 175.6 101.4 16.5 55 W HOH OH2 1157 204.0 135.5 7.7 47 W HOH OH2 1158 190.0 107.3 17.9 23 W HOH OH2 1159 177.8 144.0 24.6 23 W HOH OH2 1160 197.2 124.4 21.0 38 W HOH OH2 1161 205.9 104.1 15.4 64 W HOH OH2 1162 172.1 121.8 14.1 28 W HOH OH2 1163 194.7 144.2 17.3 48 W HOH OH2 1164 194.8 141.3 1.3 37 W HOH OH2 1165 214.8 127.8 33.0 20 W HOH OH2 1166 211.4 129.4 31.9 25 W HOH OH2 1167 179.7 121.3 11.6 45 W HOH OH2 1168 205.6 122.7 41.4 30 W HOH OH2 1169 170.3 142.8 38.0 37 W HOH OH2 1170 205.7 118.5 45.5 39 W HOH OH2 1171 203.2 121.1 3.2 49 W HOH OH2 1172 217.0 115.8 17.4 31 W HOH OH2 1173 209.1 117.1 41.6 29 W HOH OH2 1174 219.8 125.2 46.6 70 W HOH OH2 1175 157.1 125.8 36.2 39 W HOH OH2 1176 207.4 131.0 33.0 22 W HOH OH2 1177 206.9 119.2 48.3 24 W HOH OH2 1178 204.8 132.9 13.0 32 W HOH OH2 1179 191.5 101.1 25.5 37 W HOH OH2 1181 173.0 130.7 16.4 40 W HOH OH2 1182 160.9 127.1 29.4 50 W HOH OH2 1183 208.7 122.6 6.7 53 W HOH OH2 1184 215.9 121.7 17.8 45 W HOH OH2 1185 205.1 127.6 33.6 54 W HOH OH2 1186 192.8 144.2 6.3 37 W HOH OH2 1187 207.4 137.4 17.2 50 W HOH OH2 1188 213.0  90.7 38.1 44 W HOH OH2 1189 202.0 105.9 19.5 54 W HOH OH2 1190 206.1 137.8 12.7 51 W HOH OH2 1191 178.0 133.9 8.1 25 W HOH OH2 1193 187.1 141.4 31.8 38 W HOH OH2 1194 206.4 124.5 39.1 38 W HOH OH2 1195 205.8 103.3 26.3 39 W HOH OH2 1196 176.7 152.4 22.1 50 W HOH OH2 1197 188.7 114.5 13.4 38 W HOH OH2 1198 205.5 139.0 23.7 33 W HOH OH2 1200 195.1 118.4 9.4 50 W HOH OH2 1201 160.6 118.6 26.6 66 W HOH OH2 1202 186.6 122.7 13.3 31 W HOH OH2 1203 181.4 148.1 36.0 32 W HOH OH2 1204 189.7 120.4 14.1 36 W HOH OH2 1205 173.8 108.4 39.8 56 W HOH OH2 1206 217.2 123.1 19.6 39 W HOH OH2 1207 206.9 120.4 42.2 58 W HOH OH2 1208 214.1 118.3 43.6 40 W HOH OH2 1209 211.8 127.7 23.2 40 W HOH OH2 1210 194.0 117.0 16.1 34 W HOH OH2 1211 191.1 123.8 65.6 46 W HOH OH2 1212 178.7 142.5 45.3 67 W HOH OH2 1213 183.2 100.2 31.7 58 W HOH OH2 1214 212.1 121.3 11.1 54 W HOH OH2 1215 209.7 127.4 12.2 47 W HOH OH2 1216 212.0 130.9 18.8 46 W HOH OH2 1217 165.5 105.4 27.1 75 W HOH OH2 1219 191.2 122.8 6.5 32 W HOH OH2 1220 210.8 117.0 48.0 49 W HOH OH2 1221 197.1 108.2 19.0 76 W HOH OH2 1222 184.5 159.0 20.2 22 W HOH OH2 1223 215.9 128.7 24.4 73 W HOH OH2 1224 175.6 146.5 5.3 46 W HOH OH2 1225 201.5 105.4 36.8 48 W HOH OH2 1226 192.2 143.0 10.9 54 W HOH OH2 1227 157.9 122.3 39.1 54 W HOH OH2 1228 211.3 131.4 38.7 44 W HOH OH2 1229 210.5 123.4 10.2 37 W HOH OH2 1230 197.2 119.3 7.1 52 W HOH OH2 1231 175.7 141.4 29.8 22 W HOH OH2 1232 190.4 159.6 15.0 32 W HOH OH2 1233 172.3 118.7 46.4 37 W HOH OH2 1234 163.0 119.4 27.7 47 W HOH OH2 1235 208.5  98.4 26.0 46 W HOH OH2 1236 202.3 101.5 43.8 29 W HOH OH2 1237 209.7 131.9 36.2 44 W HOH OH2 1238 186.4 149.6 10.0 39 W HOH OH2 1239 212.3 126.1 13.0 42 W HOH OH2 1240 213.5 109.0 18.1 24 W HOH OH2 1241 218.2 121.1 34.8 49 W HOH OH2 1242 213.1  95.5 26.9 52 W HOH OH2 1243 193.4 146.8 23.9 46 W HOH OH2 1244 190.5 145.1 26.2 44 W HOH OH2 1245 169.6 108.8 26.2 43 W HOH OH2 1246 171.1 147.8 11.7 54 W HOH OH2 1247 195.7 109.1 48.3 45 W HOH OH2 1248 212.1 119.2 13.7 36 W HOH OH2 1249 201.7 115.2 53.9 21 W HOH OH2 1250 187.6 150.1 6.3 56 W HOH OH2 1251 217.5 128.9 31.3 73 W HOH OH2 1252 180.3 127.5 58.1 29 W HOH OH2 1253 203.4 103.2 28.9 50 W HOH OH2 1254 213.5 123.8 13.1 52 W HOH OH2 1255 197.0 116.2 17.2 56 W HOH OH2 1256 197.2 143.0 17.6 48 W HOH OH2 1257 214.2 126.4 19.1 53 W HOH OH2 1258 176.9 139.2 21.5 41 W HOH OH2 1259 183.2 159.3 23.0 52 W HOH OH2 1260 212.9 119.1 53.6 59 W HOH OH2 1261 205.0 139.0 6.1 62 W HOH OH2 1263 200.9 142.1 8.5 60 W HOH OH2 1264 203.8 135.0 26.3 55 W HOH OH2 1265 219.9 123.6 37.1 68 W HOH OH2 1266 204.8 132.5 32.4 57 W HOH OH2 1267 211.7 110.0 12.4 46 W HOH OH2 1268 193.0 114.1 17.9 46 W HOH OH2 1269 184.2  98.2 27.7 51 W HOH OH2 1270 169.9 121.7 47.4 54 W HOH OH2 1271 211.3 125.8 8.6 64 W HOH OH2 1272 181.1 141.0 48.1 56 W HOH OH2 1273 200.6 110.1 19.4 50 W HOH OH2 1274 200.4 107.9 59.1 71 W HOH OH2 1275 206.1 119.1 5.8 37 W HOH OH2 1276 207.5 116.6 5.3 55 W HOH OH2 1277 171.8 131.9 20.2 51 W HOH OH2 1278 161.6 127.9 37.2 49 W HOH OH2 1279 212.4 103.5 53.7 55 W HOH OH2 1281 221.6 113.1 44.8 66 W HOH OH2 1282 190.4 141.2 30.3 98 W HOH OH2 1283 173.0 149.1 25.5 53 W HOH OH2 1284 177.9 110.8 53.0 37 W HOH OH2 1285 204.6 116.2 43.0 39 W HOH OH2 1286 169.2 106.0 25.8 61 W HOH OH2 1287 193.1 124.4 2.4 62 W HOH OH2 1288 174.5 146.0 24.6 42 W HOH OH2 1289 197.7 112.1 26.0 34 W HOH OH2 1290 167.0 118.3 37.8 26 W HOH OH2 1291 181.5 141.2 39.8 54 W HOH OH2 1292 212.9 128.2 25.6 48 W HOH OH2 1293 191.9 134.3 1.6 39 W HOH OH2 1295 190.4 110.4 53.3 40 W HOH OH2 1296 179.3 132.2 58.2 71 W HOH OH2 1297 204.4  96.6 34.6 50 W HOH OH2 1298 211.3 121.2 56.6 51 W HOH OH2 1299 206.7 130.1 3.5 66 W HOH OH2 1300 194.9 142.4 9.7 38 W HOH OH2 1301 195.7 113.7 60.6 42 W HOH OH2 1302 180.8 112.9 47.5 46 W HOH OH2 1303 209.3 114.3 48.6 54 W HOH OH2 1304 165.3 126.6 19.8 56 W HOH OH2 1305 220.5 119.4 22.1 33 W HOH OH2 1306 179.4 133.6 10.4 37 W HOH OH2 1307 203.0 109.5 36.6 34 W HOH OH2 1308 162.5 128.4 42.1 66 W HOH OH2 1309 204.0 107.0 35.4 30 W HOH OH2 1310 198.9 119.4 54.0 45 W HOH OH2 1311 217.8 105.2 15.6 64 W HOH OH2 1312 161.1 113.3 21.3 47 W HOH OH2 1313 220.2 105.0 19.8 52 W HOH OH2 1314 214.4 111.3 16.0 36 W HOH OH2 1315 187.6 133.4 56.1 50 W HOH OH2 1316 201.7 105.0 26.4 65 W HOH OH2 1317 207.2 106.3 39.0 61 W HOH OH2 1318 191.8 112.5 55.0 49 W HOH OH2 1319 191.4 130.7 53.1 57 W HOH OH2 1320 188.7 150.9 14.6 61 W HOH OH2 1321 181.7 108.1 14.4 57 W HOH OH2 1322 194.6 147.8 17.7 67 W HOH OH2 1323 198.6  99.1 54.4 50 W HOH OH2 1324 189.6 152.7 28.0 58 W HOH OH2 1325 164.4 121.2 41.1 49 W HOH OH2 1326 207.0 131.5 36.1 46 W HOH OH2 1327 184.4 148.2 37.3 67 W HOH OH2 1328 205.2 139.2 17.7 64 W HOH OH2 1329 187.4 149.5 12.4 49 W HOH OH2 1330 191.2 122.5 11.8 53 W HOH OH2 1331 207.5 106.3 42.0 46 W HOH OH2 1332 200.4  98.8 31.5 54 W HOH OH2 1333 202.4 141.0 20.9 49 W HOH OH2 1334 187.0 125.1 5.3 68 W HOH OH2 1335 185.3 138.4 41.1 48 W HOH OH2 1336 190.2 158.5 22.6 39 W HOH OH2 1337 187.1 147.9 27.8 63 W HOH OH2 1338 203.5 140.9 23.5 68 W HOH OH2 1339 171.0 139.9 21.8 37 W HOH OH2 1340 160.0 121.8 41.7 68 W HOH OH2 1341 187.8 106.1 18.4 26 W HOH OH2 1342 174.5 128.5 13.5 58 W HOH OH2 1343 173.8 135.5 8.9 42 W HOH OH2 1344 184.7 121.5 56.7 33 W HOH OH2 1345 190.6 148.2 14.3 21 W HOH OH2 1346 194.6 121.8 4.5 76 W HOH OH2 1347 177.2 130.9 9.8 61 W HOH OH2 1348 174.1 117.7 54.2 59 W HOH OH2 1349 202.0 131.9 43.4 58 W HOH OH2 1350 175.9 138.1 18.8 40 W HOH OH2 1351 180.2 138.9 51.0 58 W HOH OH2 1352 195.7 114.6 13.2 71 W HOH OH2 1353 198.6 103.3 58.0 51 W HOH OH2 1354 187.9 144.2 31.6 47 W HOH OH2 1355 175.1 123.9 53.2 44 W HOH OH2 1356 184.6 148.8 3.9 53 W HOH OH2 1357 170.7 144.8 27.4 51 W HOH OH2 1358 168.1 142.8 19.9 74 W HOH OH2 1359 162.6 126.0 23.8 61 W HOH OH2 1360 176.3 135.9 10.0 42 W HOH OH2 1361 193.9 116.3 62.9 75 W HOH OH2 1362 178.5 109.7 14.7 70 W HOH OH2 1363 203.1 130.7 6.5 30 W HOH OH2 1364 197.2 107.5 22.5 62 W HOH OH2 1365 157.0 125.6 29.6 75 W HOH OH2 1366 203.9  96.6 38.4 70 W HOH OH2 1367 194.1 130.9 57.7 42 W HOH OH2 1368 181.4 150.1 34.0 71 W HOH OH2 1369 219.2 125.8 35.1 54 W HOH OH2 1370 188.0 145.3 28.2 47 W HOH OH2 1371 184.3 151.2 21.2 37 W HOH OH2 1372 177.0 148.7 29.3 58 W HOH OH2 1373 192.5 142.6 0.7 53 W HOH OH2 1374 214.4 125.4 44.0 30 W HOH OH2 1375 177.5 104.7 21.1 51 W HOH OH2 1376 217.5 112.6 14.0 64 W HOH OH2 1377 198.3 153.2 18.0 70 W HOH OH2 1378 184.9 145.4 1.1 57 W HOH OH2 1379 209.6 120.8 42.1 40 W HOH OH2 1380 184.6 110.5 54.9 45 W HOH OH2 1381 215.6 114.6 37.6 52 W HOH OH2 1382 213.0 122.2 16.5 45 W HOH OH2 1383 188.4 143.5 0.9 66 W HOH OH2 1384 206.5 100.8 21.4 55 W HOH OH2 1385 159.4 132.3 31.7 68 W HOH OH2 1386 174.7 147.4 28.1 52 W HOH OH2 1388 173.7 135.8 54.4 57 W HOH OH2 1389 218.4 116.4 28.3 54 W HOH OH2 1390 217.6  97.3 26.8 55 W HOH OH2 1391 176.0 126.1 15.0 54 W HOH OH2 1392 207.2 117.4 43.6 61 W HOH OH2 1393 169.0 124.7 46.2 48 W HOH OH2 1394 180.1 134.6 56.3 49 W HOH OH2 1395 170.2 108.5 29.5 47 W HOH OH2 1396 174.5 144.0 3.9 59 W HOH OH2 1397 159.9 118.6 39.2 59 W HOH OH2 1398 191.2 125.3 7.7 52 W HOH OH2 1399 212.9  93.2 39.5 53 W HOH OH2 1400 197.3 142.7 5.5 80 W HOH OH2 1401 213.6 127.4 16.6 66 W HOH OH2 1402 166.6 131.6 21.1 52 W HOH OH2 1403 204.1 132.7 27.5 67 W HOH OH2 1404 177.4 102.7 26.3 73 W HOH OH2 1405 175.4 106.5 21.8 59 W HOH OH2 1406 213.6 130.7 21.2 83 W HOH OH2 1407 215.4 129.7 26.9 69 W HOH OH2 1408 184.6 141.9 39.8 73 W HOH OH2 1409 164.1 129.3 24.3 47 W HOH OH2 1410 216.8 119.1 49.5 61 W HOH OH2 1411 211.3 118.4 42.3 43 W HOH OH2 1412 178.6 148.3 37.4 54 W HOH OH2 1413 185.9 136.4 56.0 64 W HOH OH2 1414 219.2  90.5 40.6 71 W HOH OH2 1415 208.6 131.7 13.5 39 W HOH OH2 1416 205.2 130.5 38.6 69 W HOH OH2 1417 166.1 137.4 31.9 46 W HOH OH2 1418 188.4 142.1 28.5 54 W HOH OH2 1419 207.5 134.4 32.5 60 W HOH OH2 1420 187.7 146.9 31.3 70 W HOH OH2 1421 190.3 105.4 19.8 67 W HOH OH2 1422 209.3 111.1 9.4 64 W HOH OH2 1423 203.0 134.3 59.8 85 W HOH OH2 1424 216.7 128.0 36.3 83 W HOH OH2 1425 218.3 117.1 15.5 46 W HOH OH2 1426 160.6 118.7 29.7 58 W HOH OH2 1427 175.3 133.6 7.1 46 W HOH OH2 1428 182.0 102.1 21.5 54 W HOH OH2 1429 171.9 109.5 35.5 69 W HOH OH2 1430 197.8 111.7 58.3 82 W HOH OH2 1431 184.1 105.8 11.8 52 W HOH OH2 1432 195.8 154.6 15.7 50 W HOH OH2 1433 202.6 138.8 2.4 44 W HOH OH2 1434 195.9 148.1 20.5 60 W HOH OH2 1435 204.9 111.7 54.5 50 W HOH OH2 1436 217.1 107.9 17.7 68 W HOH OH2 1437 175.5 146.3 31.1 70 W HOH OH2 1438 182.4 156.6 25.6 61 W

TABLE 5 Table 5 lists the atomic structure coordinates for FPT in complex with FPP and the inhibitor SCH69132 as derived by X-ray diffraction from crystals of that complex. The abbreviations are the same as those used in Table 2. RES ATOM # X Y Z B C GLY C 54 191.7 151.2 9.3 81 A GLY O 54 190.4 151.2 9.5 82 A GLY N 54 192.5 150.9 7.0 81 A GLY CA 54 192.2 151.9 8.0 82 A PHE N 55 192.6 150.8 10.1 81 A PHE CA 55 192.3 150.1 11.4 79 A PHE CB 55 193.2 148.9 11.6 80 A PHE CG 55 192.6 147.6 11.1 81 A PHE CD1 55 192.9 147.1 9.8 81 A PHE CD2 55 191.8 146.8 11.9 80 A PHE CE1 55 192.4 145.9 9.4 81 A PHE CE2 55 191.3 145.6 11.4 80 A PHE CZ 55 191.6 145.1 10.2 80 A PHE C 55 192.4 151.1 12.6 78 A PHE O 55 193.5 151.6 12.8 78 A LEU N 56 191.3 151.3 13.3 75 A LEU CA 56 191.4 152.1 14.5 72 A LEU CB 56 190.1 153.0 14.5 72 A LEU CG 56 190.4 154.6 14.6 72 A LEU CD1 56 189.1 155.3 14.8 72 A LEU CD2 56 191.4 154.9 15.7 72 A LEU C 56 191.5 151.3 15.8 69 A LEU O 56 190.5 150.7 16.2 69 A SER N 57 192.7 151.3 16.3 66 A SER CA 57 193.0 150.5 17.5 64 A SER CB 57 194.4 150.8 18.0 65 A SER OG 57 194.8 150.1 19.1 65 A SER C 57 192.0 150.7 18.6 62 A SER O 57 191.6 151.8 18.9 61 A LEU N 58 191.6 149.6 19.2 60 A LEU CA 58 190.7 149.6 20.4 58 A LEU CB 58 190.4 148.2 20.8 57 A LEU CG 58 188.9 147.8 20.9 56 A LEU CD1 58 188.9 146.4 21.5 57 A LEU CD2 58 188.1 148.7 21.7 55 A LEU C 58 191.3 150.4 21.5 58 A LEU O 58 190.7 150.8 22.5 59 A ASP N 59 192.6 150.6 21.4 S8 A ASP CA 59 193.5 151.3 22.4 58 A ASP CB 59 194.7 150.4 22.7 61 A ASP CG 59 194.4 149.4 23.9 64 A ASP OD1 59 194.4 148.2 23.6 65 A ASP OD2 59 194.2 149.9 25.0 66 A ASP C 59 193.9 152.7 21.9 55 A ASP O 59 194.5 153.4 22.7 55 A SER N 60 193.7 153.0 20.7 51 A SER CA 60 194.1 154.2 20.1 48 A SER CB 60 193.5 154.3 18.7 48 A SER OG 60 193.8 155.6 18.2 49 A SER C 60 193.5 155.3 21.0 46 A SER O 60 192.4 155.2 21.5 47 A PRO N 61 194.3 156.4 21.2 44 A PRO CD 61 195.7 156.6 20.7 44 A PRO CA 61 193.8 157.5 22.1 43 A PRO CB 61 195.1 158.3 22.2 43 A PRO CG 61 195.8 158.1 20.9 43 A PRO C 61 192.7 158.2 21.4 42 A PRO O 61 191.8 158.8 22.0 42 A THR N 62 192.7 158.1 20.0 40 A THR CA 62 191.7 158.8 19.2 40 A THR CB 62 192.4 159.5 18.0 40 A THR OG1 62 193.1 158.5 17.2 39 A THR CG2 62 193.4 160.5 18.4 39 A THR C 62 190.6 157.8 18.7 40 A THR O 62 189.9 158.1 17.7 42 A TYR N 63 190.4 156.7 19.4 39 A TYR CA 63 189.4 155.7 19.0 37 A TYR CB 63 189.7 154.4 19.8 36 A TYR CG 63 188.6 153.3 19.7 36 A TYR CD1 63 188.6 152.4 18.6 36 A TYR CE1 63 187.6 151.4 18.5 36 A TYR CD2 63 187.6 153.3 20.6 36 A TYR CE2 63 186.5 152.3 20.5 35 A TYR CZ 63 186.6 151.4 19.5 36 A TYR OH 63 185.5 150.5 19.4 35 A TYR C 63 188.0 156.2 19.4 35 A TYR O 63 187.8 156.8 20.4 35 A VAL N 64 187.1 156.1 18.4 34 A VAL CA 64 185.7 156.6 18.6 34 A VAL CB 64 185.4 157.7 17.6 34 A VAL CG1 64 186.2 159.0 17.8 33 A VAL CG2 64 185.6 157.2 16.1 34 A VAL C 64 184.7 155.4 18.6 34 A VAL O 64 185.0 154.4 17.9 35 A LEU N 65 183.6 155.6 19.3 34 A LEU CA 65 182.6 154.5 19.3 33 A LEU CB 65 181.5 154.9 20.3 29 A LEU CG 65 181.9 155.0 21.8 28 A LEU CD1 65 180.7 155.2 22.7 28 A LEU CD2 65 182.6 153.7 22.2 27 A LEU C 65 182.0 154.3 18.0 35 A LEU O 65 181.8 155.3 17.2 37 A TYR N 66 181.6 153.1 17.6 37 A TYR CA 66 181.1 152.8 16.3 38 A TYR CB 66 180.7 151.3 16.2 37 A TYR CG 66 181.8 150.5 15.8 36 A TYR CD1 66 182.7 150.1 16.8 35 A TYR CE1 66 183.9 149.4 16.5 35 A TYR CD2 66 182.1 150.2 14.5 35 A TYR CE2 66 183.3 149.5 14.2 35 A TYR CZ 66 184.2 149.1 15.2 35 A TYR OH 66 185.3 148.5 14.8 34 A TYR C 66 179.9 153.7 15.9 39 A TYR O 66 179.7 154.1 14.8 39 A ARG N 67 179.1 154.1 16.9 42 A ARG CA 67 177.9 154.9 16.7 45 A ARG CB 67 177.0 155.0 17.9 45 A ARG CG 67 177.6 155.7 19.2 47 A ARG CD 67 176.5 155.8 20.3 48 A ARG NE 67 177.0 156.2 21.5 49 A ARG CZ 67 177.3 155.5 22.6 50 A ARG NH1 67 177.0 154.1 22.5 51 A ARG NH2 67 177.8 156.0 23.7 50 A ARG C 67 178.3 156.3 16.3 46 A ARG O 67 177.5 157.0 15.7 47 A ASP N 68 179.5 156.8 16.6 45 A ASP CA 68 179.9 158.1 16.3 45 A ASP CB 68 180.9 158.7 17.3 44 A ASP CG 68 180.1 159.0 18.6 44 A ASP OD1 68 178.9 159.2 18.6 44 A ASP OD2 68 180.8 159.1 19.7 43 A ASP C 68 180.7 158.1 14.9 46 A ASP O 68 181.3 159.0 14.5 46 A ARG N 69 180.6 156.9 14.3 47 A ARG CA 69 181.3 156.7 13.0 48 A ARG CB 69 182.0 155.3 13.0 48 A ARG CG 69 182.9 155.1 14.2 47 A ARG CD 69 183.8 153.9 13.9 45 A ARG NE 69 184.7 153.5 15.1 43 A ARG CZ 69 185.7 152.6 15.0 43 A ARG NH1 69 186.0 152.1 13.9 42 A ARG NH2 69 186.3 152.3 16.1 43 A ARG C 69 180.4 156.9 11.7 50 A ARG O 69 179.4 156.2 11.5 51 A ALA N 70 180.9 157.7 10.8 52 A ALA CA 70 180.2 158.1 9.6 53 A ALA CB 70 180.9 159.3 8.9 54 A ALA C 70 180.0 156.9 8.5 54 A ALA O 70 179.2 157.0 7.7 56 A GLU N 71 180.9 155.9 8.6 55 A GLU CA 71 180.8 154.8 7.7 55 A GLU CB 71 182.2 154.3 7.3 55 A GLU CG 71 183.1 153.8 8.5 57 A GLU CD 71 183.5 154.9 9.5 57 A GLU OE1 71 183.7 154.6 10.7 57 A GLU OE2 71 183.5 156.1 9.1 58 A GLU C 71 180.0 153.7 8.4 55 A GLU O 71 179.9 152.6 7.8 53 A TRP N 72 179.4 154.0 9.5 55 A TRP CA 72 178.6 153.1 10.3 57 A TRP CB 72 179.4 152.7 11.6 56 A TRP CG 72 180.4 151.7 11.4 55 A TRP CD2 72 180.2 150.3 11.2 54 A TRP CE2 72 181.5 149.7 11.1 54 A TRP CE3 72 179.1 149.5 11.2 54 A TRP CD1 72 181.8 151.9 11.4 55 A TRP NE1 72 182.4 150.7 11.2 55 A TRP CZ2 72 181.6 148.3 10.9 54 A TRP CZ3 72 179.2 148.1 11.0 54 A TRP CH2 72 180.5 147.5 10.8 54 A TRP C 72 177.3 153.7 10.7 59 A TRP O 72 176.5 153.1 11.4 59 A ALA N 73 177.0 154.9 10.2 60 A ALA CA 73 175.7 155.6 10.5 62 A ALA CB 73 175.9 157.1 10.4 62 A ALA C 73 174.5 155.1 9.7 62 A ALA O 73 173.4 155.4 10.0 63 A ASP N 74 174.8 154.3 8.6 62 A ASP CA 74 173.8 153.8 7.8 62 A ASP CB 74 174.4 153.5 6.4 62 A ASP CG 74 175.3 152.3 6.5 62 A ASP OD1 74 175.0 151.2 5.9 62 A ASP OD2 74 176.4 152.4 7.1 61 A ASP C 74 173.2 152.6 8.4 62 A ASP O 74 172.0 152.3 8.1 63 A ILE N 75 173.9 151.9 9.2 61 A ILE CA 75 173.5 150.6 9.9 60 A ILE CB 75 174.5 149.5 9.8 59 A ILE CG2 75 175.7 149.8 10.7 59 A ILE CG1 75 173.9 148.2 10.1 59 A ILE CD1 75 174.8 147.0 9.8 60 A ILE C 75 173.0 150.8 11.3 60 A ILE O 75 173.5 151.6 12.0 61 A ASP N 76 171.9 150.1 11.7 60 A ASP CA 76 171.3 150.2 13.0 59 A ASP CB 76 169.8 150.0 12.9 62 A ASP CG 76 169.0 151.3 12.9 64 A ASP OD1 76 169.2 152.1 12.0 65 A ASP OD2 76 168.2 151.5 13.8 64 A ASP C 76 171.9 149.2 14.0 57 A ASP O 76 171.8 148.0 13.7 56 A PRO N 77 172.4 149.6 15.1 55 A PRO CD 77 172.7 151.0 15.4 55 A PRO CA 77 173.0 148.7 16.1 54 A PRO CB 77 173.6 149.6 17.1 54 A PRO CG 77 172.9 150.9 16.9 54 A PRO C 77 171.8 147.9 16.7 53 A PRO O 77 170.7 148.4 17.0 53 A VAL N 78 172.1 146.7 17.0 52 A VAL CA 78 171.1 145.8 17.6 51 A VAL CB 78 171.0 144.5 16.9 51 A VAL CG1 78 170.0 143.5 17.5 51 A VAL CG2 78 170.7 144.7 15.4 51 A VAL C 78 171.5 145.5 19.1 52 A VAL O 78 172.5 144.7 19.3 53 A PRO N 79 170.9 146.1 20.0 51 A PRO CD 79 169.8 147.2 19.9 51 A PRO CA 79 171.2 145.9 21.5 51 A PRO CB 79 170.4 147.0 22.2 51 A PRO CG 79 169.2 147.1 21.3 51 A PRO C 79 170.8 144.5 21.9 50 A PRO O 79 169.9 143.9 21.4 49 A GLN N 80 171.6 144.0 22.9 50 A GLN CA 80 171.4 142.7 23.4 50 A GLN CB 80 172.5 142.2 24.4 48 A GLN CG 80 172.4 140.8 24.8 47 A GLN CD 80 173.7 140.2 25.3 46 A GLN OE1 80 174.4 139.6 24.6 46 A GLN NE2 80 174.0 140.5 26.6 47 A GLN C 80 170.0 142.5 24.2 51 A GLN O 80 169.6 143.4 24.9 52 A ASN N 81 169.4 141.4 24.0 52 A ASN CA 81 168.1 141.1 24.6 53 A ASN CB 81 167.1 140.6 23.5 53 A ASN CG 81 165.8 140.3 24.1 54 A ASN OD1 81 165.4 140.7 25.3 53 A ASN ND2 81 165.0 139.5 23.4 54 A ASN C 81 168.3 140.0 25.7 53 A ASN O 81 168.2 138.8 25.4 52 A ASP N 82 168.5 140.5 26.9 54 A ASP CA 82 168.6 139.6 28.1 55 A ASP CB 82 169.5 140.2 29.1 56 A ASP CG 82 171.0 140.1 28.7 56 A ASP OD1 82 171.3 139.5 27.7 55 A ASP OD2 82 171.8 140.7 29.4 56 A ASP C 82 167.3 139.3 28.7 56 A ASP O 82 167.2 138.6 29.7 56 A GLY N 83 166.2 139.9 28.1 57 A GLY CA 83 164.9 139.7 28.6 58 A GLY C 83 164.5 140.8 29.6 59 A GLY O 83 165.3 141.6 30.1 60 A PRO N 84 163.2 140.9 29.8 58 A PRO CD 84 162.1 140.1 29.3 58 A PRO CA 84 162.6 141.9 30.7 58 A PRO CB 84 161.1 141.6 30.7 58 A PRO CG 84 161.1 140.2 30.4 58 A PRO C 84 163.2 141.8 32.1 57 A PRO O 84 163.4 142.9 32.8 57 A SER N 85 163.5 140.6 32.6 56 A SER CA 85 164.0 140.4 33.9 55 A SER CB 85 163.0 139.6 34.8 56 A SER OG 85 161.8 140.4 34.8 58 A SER C 85 165.3 139.5 33.8 54 A SER O 85 165.2 138.3 33.9 54 A PRO N 86 166.4 140.2 33.6 52 A PRO CD 86 166.5 141.6 33.4 52 A PRO CA 86 167.8 139.6 33.4 51 A PRO CB 86 168.6 140.9 33.3 52 A PRO CG 86 167.7 141.8 32.6 52 A PRO C 86 168.3 138.7 34.6 48 A PRO O 86 167.7 138.7 35.7 48 A VAL N 87 169.3 138.0 34.3 46 A VAL CA 87 170.0 137.1 35.3 43 A VAL CB 87 169.4 135.7 35.3 43 A VAL CG1 87 168.4 135.6 36.4 43 A VAL CG2 87 168.9 135.3 34.0 42 A VAL C 87 171.5 137.1 34.8 41 A VAL O 87 171.7 137.3 33.6 40 A VAL N 88 172.4 136.8 35.7 38 A VAL CA 88 173.8 136.8 35.4 36 A VAL CB 88 174.4 135.4 35.1 35 A VAL CG1 88 174.3 134.5 36.3 35 A VAL CG2 88 173.8 134.8 33.9 35 A VAL C 88 174.1 137.8 34.3 36 A VAL O 88 174.8 137.5 33.3 38 A GLN N 89 173.6 139.0 34.5 35 A GLN CA 89 173.7 140.1 33.6 34 A GLN CB 89 172.6 141.1 33.8 34 A GLN CG 89 172.8 142.4 33.1 35 A GLN CD 89 171.8 143.4 33.4 35 A GLN OE1 89 171.4 143.7 34.6 36 A GLN NE2 89 171.1 143.9 32.3 35 A GLN C 89 175.1 140.9 33.8 35 A GLN O 89 175.4 141.2 34.9 36 A ILE N 90 175.7 141.2 32.7 34 A ILE CA 90 177.0 141.8 32.7 34 A ILE CB 90 178.0 141.2 31.8 33 A ILE CG2 90 179.4 141.8 31.9 33 A ILE CG1 90 178.2 139.7 32.1 32 A ILE CD1 90 178.8 138.9 30.9 31 A ILE C 90 176.9 143.3 32.5 34 A ILE O 90 176.3 143.7 31.5 35 A ILE N 91 177.4 144.2 33.3 35 A ILE CA 91 177.4 145.6 33.1 35 A ILE CB 91 177.5 146.4 34.5 35 A ILE CG2 91 177.5 147.9 34.2 35 A ILE CG1 91 176.3 146.0 35.4 35 A ILE CD1 91 174.9 146.4 34.8 35 A ILE C 91 178.5 146.0 32.2 35 A ILE O 91 179.5 146.5 32.6 35 A TYR N 92 178.2 145.8 30.9 35 A TYR CA 92 179.2 146.1 29.9 37 A TYR CB 92 178.7 145.8 28.5 35 A TYR CG 92 178.1 144.5 28.3 35 A TYR CD1 92 176.8 144.3 27.8 35 A TYR CE1 92 176.2 143.1 27.6 35 A TYR CD2 92 178.8 143.3 28.6 34 A TYR CE2 92 178.2 142.0 28.5 35 A TYR CZ 92 176.9 141.9 28.0 35 A TYR OH 92 176.3 140.7 27.9 34 A TYR C 92 179.7 147.5 29.9 38 A TYR O 92 179.0 148.4 30.4 38 A SER N 93 180.9 147.7 29.4 40 A SER CA 93 181.5 149.0 29.4 41 A SER CB 93 183.0 148.9 29.1 41 A SER OG 93 183.2 148.1 27.9 42 A SER C 93 180.8 149.6 28.2 42 A SER O 93 179.9 149.0 27.5 43 A GLU N 94 181.1 150.8 27.8 44 A GLU CA 94 180.5 151.5 26.7 45 A GLU CB 94 180.8 153.0 26.8 48 A GLU CG 94 180.1 153.8 25.6 50 A GLU CD 94 178.9 154.5 26.1 52 A GLU OE1 94 177.9 153.9 26.5 52 A GLU OE2 94 179.0 155.8 26.1 53 A GLU C 94 181.0 151.0 25.4 45 A GLU O 94 180.2 151.0 24.4 44 A LYS N 95 182.3 150.8 25.3 44 A LYS CA 95 183.0 150.3 24.1 43 A LYS CB 95 184.5 150.3 24.2 44 A LYS CG 95 185.1 151.7 24.6 45 A LYS CD 95 186.5 151.5 25.1 46 A LYS CE 95 187.5 150.9 24.1 47 A LYS NZ 95 188.8 150.5 24.6 47 A LYS C 95 182.5 148.9 23.8 42 A LYS O 95 182.2 148.6 22.7 42 A PHE N 96 182.6 148.0 24.9 40 A PHE CA 96 182.3 146.6 24.7 38 A PHE CB 96 182.3 145.9 26.1 36 A PHE CG 96 182.1 144.5 26.0 36 A PHE CD1 96 183.1 143.6 26.1 35 A PHE CD2 96 180.8 143.9 25.7 35 A PHE CE1 96 182.9 142.2 26.0 34 A PHE CE2 96 180.6 142.6 25.6 34 A PHE CZ 96 181.7 141.7 25.7 34 A PHE C 96 180.9 146.6 24.2 40 A PHE O 96 180.6 146.1 23.1 40 A ARG N 97 179.9 147.2 24.9 41 A ARG CA 97 178.5 147.3 24.5 43 A ARG CB 97 177.7 148.1 25.4 44 A ARG CG 97 176.3 147.7 25.6 48 A ARG CD 97 175.4 148.9 26.0 51 A ARG NE 97 176.0 149.7 27.1 53 A ARG CZ 97 176.6 150.8 26.9 55 A ARG NH1 97 176.8 151.3 25.6 56 A ARG NH2 97 177.1 151.5 27.9 56 A ARG C 97 178.4 147.9 23.1 42 A ARG O 97 177.6 147.4 22.2 44 A ASP N 98 179.1 149.0 22.8 42 A ASP CA 98 179.1 149.6 21.5 41 A ASP CB 98 180.0 150.9 21.5 41 A ASP CG 98 180.1 151.6 20.1 40 A ASP OD1 98 179.1 152.3 19.8 41 A ASP OD2 98 181.1 151.3 19.4 39 A ASP C 98 179.5 148.7 20.3 40 A ASP O 98 178.7 148.6 19.3 41 A VAL N 99 180.6 148.0 20.4 38 A VAL CA 99 181.1 147.1 19.4 35 A VAL CB 99 182.5 146.5 19.7 33 A VAL CG1 99 182.9 145.4 18.8 32 A VAL CG2 99 183.5 147.6 19.7 33 A VAL C 99 180.2 145.9 19.1 34 A VAL O 99 179.9 145.5 18.0 33 A TYR N 100 179.6 145.4 20.2 33 A TYR CA 100 178.7 144.3 20.2 32 A TYR CB 100 178.7 143.6 21.5 30 A TYR CG 100 179.8 142.6 21.5 28 A TYR CD1 100 180.9 142.9 22.2 27 A TYR CE1 100 182.0 142.0 22.1 26 A TYR CD2 100 179.7 141.4 20.8 28 A TYR CE2 100 180.7 140.6 20.7 27 A TYR CZ 100 181.9 140.8 21.4 27 A TYR OH 100 182.9 139.9 21.3 26 A TYR C 100 177.4 144.6 19.6 34 A TYR O 100 176.9 143.9 18.7 35 A ASP N 101 176.8 145.7 20.0 35 A ASP CA 101 175.5 146.1 19.4 35 A ASP CB 101 175.1 147.5 19.8 37 A ASP CG 101 174.5 147.5 21.2 38 A ASP OD1 101 174.5 146.5 21.9 38 A ASP OD2 101 174.0 148.6 21.6 39 A ASP C 101 175.7 146.2 17.9 35 A ASP O 101 174.8 145.8 17.1 35 A TYR N 102 176.9 146.7 17.5 35 A TYR CA 102 177.1 146.7 16.0 37 A TYR CB 102 178.2 147.7 15.7 39 A TYR CG 102 177.7 149.1 15.3 40 A TYR CD1 102 177.3 149.4 14.0 40 A TYR CE1 102 176.7 150.6 13.7 41 A TYR CD2 102 177.4 150.0 16.3 40 A TYR CE2 102 176.8 151.2 16.0 40 A TYR CZ 102 176.5 151.5 14.7 41 A TYR OH 102 175.8 152.7 14.4 41 A TYR C 102 177.4 145.3 15.5 37 A TYR O 102 177.1 145.1 14.3 36 A PHE N 103 178.0 144.4 16.3 37 A PHE CA 103 178.3 143.1 15.8 37 A PHE CB 103 179.1 142.2 16.7 36 A PHE CG 103 179.4 140.8 16.2 34 A PHE CD1 103 180.3 140.5 15.2 34 A PHE CD2 103 178.7 139.7 16.8 33 A PHE CE1 103 180.5 139.2 14.7 32 A PHE CE2 103 178.9 138.4 16.3 31 A PHE CZ 103 179.8 138.2 15.2 31 A PHE C 103 176.9 142.4 15.5 40 A PHE O 103 176.7 141.9 14.4 41 A ARG N 104 176.0 142.4 16.5 40 A ARG CA 104 174.7 141.8 16.3 41 A ARG CB 104 173.8 142.1 17.4 42 A ARG CG 104 174.2 141.5 18.7 42 A ARG CD 104 173.3 141.9 19.8 43 A ARG NE 104 174.0 141.6 21.1 45 A ARG CZ 104 174.7 142.5 21.8 46 A ARG NH1 104 174.9 143.7 21.4 47 A ARG NH2 104 175.3 142.0 22.9 47 A ARG C 104 174.1 142.3 15.0 41 A ARG O 104 173.6 141.5 14.2 41 A ALA N 105 174.2 143.6 14.8 42 A ALA CA 105 173.6 144.3 13.6 42 A ALA CB 105 174.0 145.7 13.6 42 A ALA C 105 174.1 143.6 12.3 42 A ALA O 105 173.3 143.2 11.5 43 A VAL N 106 175.4 143.6 12.2 42 A VAL CA 106 176.1 143.1 11.0 43 A VAL CB 106 177.6 143.5 11.0 43 A VAL CG1 106 178.6 142.3 10.9 44 A VAL CG2 106 177.9 144.6 10.0 43 A VAL C 106 176.0 141.6 10.8 43 A VAL O 106 175.8 141.1 9.7 42 A LEU N 107 176.0 140.8 12.0 43 A LEU CA 107 175.8 139.4 11.9 44 A LEU CB 107 176.1 138.B 13.3 43 A LEU CG 107 175.9 137.3 13.5 42 A LEU CD1 107 176.9 136.6 12.5 41 A LEU CD2 107 176.1 136.8 14.9 40 A LEU C 107 174.4 139.1 11.5 47 A LEU O 107 174.2 138.2 10.7 47 A GLN N 108 173.5 139.8 12.1 50 A GLN CA 108 172.1 139.7 11.9 53 A GLN CB 108 171.3 141.0 12.5 56 A GLN CG 108 170.0 140.7 13.2 58 A GLN CD 108 170.2 140.5 14.7 60 A GLN OE1 108 169.4 140.9 15.5 61 A GLN NE2 108 171.4 139.9 15.1 60 A GLN C 108 171.8 139.7 10.4 54 A GLN O 108 171.3 138.7 9.9 55 A ARG N 109 172.2 140.7 9.7 54 A ARG CA 109 172.0 140.8 8.3 54 A ARG CB 109 172.0 142.2 7.8 56 A ARG CG 109 173.3 142.9 8.1 59 A ARG CD 109 173.2 144.4 7.6 61 A ARG NE 109 172.2 145.1 B.4 63 A ARG CZ 109 171.6 146.2 7.9 65 A ARG NH1 109 171.9 146.6 6.7 66 A ARG NH2 109 170.7 146.8 8.6 65 A ARG C 109 173.0 140.0 7.5 52 A ARG O 109 173.0 139.9 6.3 52 A ASP N 110 173.9 139.3 8.2 50 A ASP CA 110 175.0 138.5 7.6 49 A ASP CB 110 174.4 137.2 7.0 49 A ASP CG 110 175.5 136.3 6.4 50 A ASP OD1 110 176.6 136.2 7.0 50 A ASP OD2 110 175.2 135.7 5.4 51 A ASP C 110 175.6 139.4 6.6 48 A ASP O 110 175.7 139.0 5.4 47 A GLU N 111 176.1 140.5 7.0 48 A GLU CA 111 176.8 141.5 6.1 47 A GLU CB 111 176.7 142.9 6.8 48 A GLU CG 111 177.0 144.0 5.9 48 A GLU CD 111 177.2 145.3 6.7 49 A GLU OE1 111 178.4 145.8 6.6 48 A GLU OE2 111 176.3 145.8 7.3 49 A GLU C 111 178.2 141.0 6.0 47 A GLU O 111 179.0 141.1 7.0 47 A ARG N 112 178.6 140.5 4.9 46 A ARG CA 112 179.9 140.0 4.6 45 A ARG CB 112 179.9 138.7 3.8 45 A ARG CG 112 179.0 137.7 4.4 46 A ARG CD 112 178.9 136.4 3.7 47 A ARG NE 112 178.0 135.5 4.4 49 A ARG CZ 112 177.8 134.2 4.2 50 A ARG NH1 112 178.5 133.6 3.3 50 A ARG NH2 112 176.9 133.6 4.9 50 A ARG C 112 180.8 141.1 4.0 44 A ARG O 112 181.3 141.0 2.9 43 A SER N 113 181.0 142.2 4.8 44 A SER CA 113 181.7 143.3 4.3 44 A SER CB 113 180.9 144.6 4.5 43 A SER OG 113 180.8 145.0 5.9 42 A SER C 113 183.1 143.5 5.0 44 A SER O 113 183.3 143.0 6.1 45 A GLU N 114 184.0 144.2 4.3 44 A GLU CA 114 185.3 144.5 4.8 44 A GLU CB 114 186.0 145.4 3.8 45 A GLU CG 114 187.3 145.9 4.2 47 A GLU CD 114 188.3 144.9 4.4 49 A GLU OE1 114 189.1 145.0 5.4 50 A GLU OE2 114 188.3 143.9 3.6 50 A GLU C 114 185.2 145.2 6.2 44 A GLU O 114 186.1 145.1 7.0 44 A ARG N 115 184.2 146.0 6.4 44 A ARG CA 115 184.0 146.7 7.6 44 A ARG CB 115 183.0 147.9 7.5 44 A ARG CG 115 181.7 147.5 7.0 45 A ARG CD 115 180.8 148.7 7.1 47 A ARG NE 115 179.4 148.4 6.8 48 A ARG CZ 115 178.3 149.2 7.1 49 A ARG NH1 115 177.1 148.7 6.8 50 A ARG NH2 115 178.4 150.3 7.7 49 A ARG C 115 183.5 145.7 8.7 44 A ARG O 115 183.9 145.8 9.9 45 A ALA N 116 182.7 144.8 8.3 43 A ALA CA 116 182.2 143.8 9.3 41 A ALA CB 116 181.2 142.8 8.6 40 A ALA C 116 183.5 143.0 9.7 41 A ALA O 116 183.6 142.6 10.8 41 A PHE N 117 184.4 142.8 8.7 39 A PHE CA 117 185.6 142.1 8.9 37 A PHE CB 117 186.4 141.9 7.6 35 A PHE CG 117 187.8 141.3 7.8 34 A PHE CD1 117 187.9 140.0 8.2 33 A PHE CD2 117 188.9 142.0 7.7 34 A PHE CE1 117 189.1 139.4 8.4 32 A PHE CE2 117 190.2 141.4 7.9 32 A PHE CZ 117 190.3 140.1 8.3 32 A PHE C 117 186.5 142.9 9.9 36 A PHE O 117 187.0 142.2 10.8 37 A LYS N 118 186.6 144.2 9.8 34 A LYS CA 118 187.4 145.0 10.8 32 A LYS CB 118 187.6 146.3 10.2 34 A LYS CG 118 188.6 146.3 9.0 36 A LYS CD 118 189.2 147.7 8.8 37 A LYS CE 118 190.0 147.8 7.5 39 A LYS NZ 118 189.2 147.6 6.3 39 A LYS C 118 186.7 145.1 12.1 31 A LYS O 118 187.4 145.2 13.1 31 A LEU N 119 185.4 145.0 12.2 30 A LEU CA 119 184.7 145.1 13.5 29 A LEU CB 119 183.2 145.4 13.3 28 A LEU CG 119 182.3 145.2 14.6 27 A LEU CD1 119 182.6 146.4 15.5 27 A LEU CD2 119 180.9 145.2 14.2 27 A LEU C 119 184.9 143.8 14.3 30 A LEU O 119 185.0 143.9 15.6 30 A THR N 120 184.9 142.7 13.7 30 A THR CA 120 185.1 141.4 14.4 29 A THR CB 120 185.2 140.2 13.5 29 A THR OG1 120 186.2 140.4 12.6 28 A THR CG2 120 183.9 140.0 12.8 29 A THR C 120 186.4 141.5 15.2 29 A THR O 120 186.5 141.0 16.3 30 A ARG N 121 187.4 142.1 14.6 29 A ARG CA 121 188.7 142.2 15.3 31 A ARG CB 121 189.7 142.9 14.5 31 A ARG CG 121 191.0 143.1 15.2 34 A ARG CD 121 191.8 144.2 14.7 37 A ARG NE 121 192.6 143.7 13.7 40 A ARG CZ 121 193.9 144.0 13.6 42 A ARG NH1 121 194.7 143.5 12.6 44 A ARG NH2 121 194.4 144.8 14.5 43 A ARG C 121 188.6 142.9 16.6 32 A ARG O 121 189.2 142.5 17.6 33 A ASP N 122 187.7 143.9 16.7 32 A ASP CA 122 187.5 144.7 17.9 31 A ASP CB 122 186.8 146.0 17.6 31 A ASP CG 122 187.8 147.1 17.1 31 A ASP OD1 122 189.0 146.9 17.3 32 A ASP OD2 122 187.3 148.1 16.6 32 A ASP C 122 186.6 143.9 18.9 31 A ASP O 122 186.8 143.9 20.1 30 A ALA N 123 185.7 143.1 18.4 30 A ALA CA 123 184.8 142.3 19.1 30 A ALA CB 123 183.7 141.7 18.3 30 A ALA C 123 185.6 141.1 19.7 30 A ALA O 123 185.4 140.7 20.9 32 A ILE N 124 186.6 140.7 19.0 30 A ILE CA 124 187.5 139.6 19.4 28 A ILE CB 124 188.3 139.1 18.3 27 A ILE CG2 124 189.6 138.4 18.8 27 A ILE CG1 124 187.5 138.1 17.4 26 A ILE CD1 124 188.2 137.7 16.1 26 A ILE C 124 188.4 140.1 20.5 28 A ILE O 124 188.6 139.5 21.5 28 A GLU N 125 188.9 141.3 20.3 29 A GLU CA 125 189.8 141.9 21.3 31 A GLU CB 125 190.3 143.3 20.9 35 A GLU CG 125 191.8 143.4 20.5 41 A GLU CD 125 192.2 144.8 20.1 45 A GLU OE1 125 192.9 145.5 20.9 47 A GLU OE2 125 191.9 145.3 19.0 46 A GLU C 125 189.0 142.1 22.6 30 A GLU O 125 189.6 141.9 23.7 30 A LEU N 126 187.7 142.5 22.5 29 A LEU CA 126 186.9 142.7 23.7 26 A LEU CB 126 185.6 143.5 23.3 25 A LEU CG 126 185.8 144.9 22.9 24 A LEU CD1 126 184.5 145.5 22.4 24 A LEU CD2 126 186.3 145.8 24.1 23 A LEU C 126 186.6 141.4 24.4 25 A LEU O 126 186.4 141.4 25.6 25 A ASN N 127 186.5 140.3 23.7 24 A ASN CA 127 186.2 139.0 24.3 23 A ASN CB 127 184.7 138.9 24.6 22 A ASN CG 127 184.5 137.6 25.2 23 A ASN OD1 127 185.4 136.9 25.8 24 A ASN ND2 127 183.2 137.1 25.2 24 A ASN C 127 186.7 137.9 23.4 24 A ASN O 127 185.9 137.4 22.6 25 A ALA N 128 188.0 137.7 23.5 23 A ALA CA 128 188.6 136.7 22.6 23 A ALA CB 128 190.1 136.6 22.9 22 A ALA C 128 188.0 135.3 22.7 23 A ALA O 128 188.4 134.4 21.9 24 A ALA N 129 187.2 135.0 23.6 22 A ALA CA 129 186.6 133.7 23.8 21 A ALA CB 129 186.5 133.4 25.2 21 A ALA C 129 185.2 133.6 23.2 21 A ALA O 129 184.5 132.6 23.3 21 A ASN N 130 184.8 134.7 22.5 21 A ASN CA 130 183.5 134.7 21.8 20 A ASN CB 130 183.0 136.1 21.6 22 A ASN CG 130 181.6 136.1 21.2 24 A ASN OD1 130 181.1 135.3 20.5 26 A ASN ND2 130 180.9 137.1 21.8 24 A ASN C 130 183.7 133.9 20.5 20 A ASN O 130 184.1 134.4 19.5 20 A TYR N 131 183.4 132.6 20.6 20 A TYR CA 131 183.5 131.7 19.5 20 A TYR CB 131 183.2 130.2 19.9 18 A TYR CG 131 181.9 130.0 20.5 18 A TYR CD1 131 180.8 129.6 19.8 18 A TYR CE1 131 179.5 129.5 20.3 17 A TYR CD2 131 181.7 130.3 21.9 17 A TYR CE2 131 180.4 130.2 22.4 17 A TYR CZ 131 179.3 129.8 21.7 18 A TYR OH 131 178.1 129.8 22.3 19 A TYR C 131 182.5 132.0 18.3 20 A TYR O 131 182.7 131.5 17.2 22 A THR N 132 181.5 132.8 18.5 21 A THR CA 132 180.6 133.2 17.5 20 A THR CB 132 179.2 133.8 18.0 21 A THR OG1 132 178.5 132.8 18.8 20 A THR CG2 132 178.4 134.2 16.9 21 A THR C 132 181.2 134.2 16.6 21 A THR O 132 181.1 134.1 15.4 23 A VAL N 133 181.9 135.1 17.2 22 A VAL CA 133 182.6 136.2 16.4 23 A VAL CB 133 183.2 137.3 17.3 24 A VAL CG1 133 183.9 138.3 16.4 23 A VAL CG2 133 182.1 138.0 18.1 23 A VAL C 133 183.7 135.5 15.6 24 A VAL O 133 183.8 135.7 14.4 27 A TRP N 134 184.4 134.6 16.2 24 A TRP CA 134 185.5 133.8 15.5 24 A TRP CB 134 186.2 132.9 16.5 21 A TRP CG 134 187.2 133.5 17.4 20 A TRP CD2 134 188.5 134.0 17.0 19 A TRP CE2 134 189.2 134.5 18.1 18 A TRP CE3 134 189.2 134.1 15.7 19 A TRP CD1 134 187.2 133.7 18.7 19 A TRP NE1 134 188.3 134.4 19.2 18 A TRP CZ2 134 190.4 135.1 18.1 18 A TRP CZ3 134 190.4 134.6 15.7 19 A TRP CH2 134 191.0 135.1 16.8 19 A TRP C 134 185.0 133.1 14.3 26 A TRP O 134 185.6 133.0 13.3 26 A HIS N 135 183.8 132.5 14.4 29 A HIS CA 135 183.1 131.8 13.3 31 A HIS CB 135 181.9 131.1 13.8 33 A HIS CG 135 181.1 130.5 12.7 34 A HIS CD2 135 180.2 131.0 11.8 34 A HIS ND1 135 181.2 129.1 12.4 34 A HIS CE1 135 180.5 128.8 11.3 35 A HIS NE2 135 179.9 130.0 11.0 35 A HIS C 135 182.8 132.8 12.2 31 A HIS O 135 183.3 132.5 11.1 31 A PHE N 136 182.1 133.8 12.5 31 A PHE CA 136 181.7 134.8 11.5 30 A PHE CB 136 180.9 136.0 12.1 32 A PHE CG 136 180.3 136.9 11.1 35 A PHE CD1 136 179.4 136.5 10.1 35 A PHE CD2 136 180.8 138.3 11.0 35 A PHE CE1 136 178.9 137.3 9.1 34 A PHE CE2 136 180.2 139.1 10.0 35 A PHE CZ 136 179.3 138.6 9.1 35 A PHE C 136 183.0 135.4 10.8 30 A PHE O 136 183.1 135.5 9.6 31 A ARG N 137 184.1 135.6 11.6 28 A ARG CA 137 185.3 136.1 11.0 25 A ARG CB 137 186.4 136.3 12.1 24 A ARG CG 137 187.7 136.9 11.5 21 A ARG CD 137 188.6 137.3 12.6 20 A ARG NE 137 189.9 137.8 12.0 19 A ARG CZ 137 190.2 139.1 11.9 20 A ARG NH1 137 189.3 140.0 12.3 18 A ARG NH2 137 191.4 139.4 11.4 20 A ARG C 137 185.9 135.0 10.0 26 A ARG O 137 186.3 135.4 8.9 27 A ARG N 138 185.9 133.8 10.3 26 A ARG CA 138 186.4 132.8 9.3 25 A ARG CB 138 186.4 131.4 9.9 24 A ARG CG 138 187.7 130.7 9.9 22 A ARG CD 138 188.2 130.5 11.3 21 A ARG NE 138 187.3 129.7 12.1 21 A ARG CZ 138 187.2 129.6 13.4 20 A ARG NH1 138 188.0 130.4 14.1 21 A ARG NH2 138 186.4 128.8 14.0 19 A ARG C 138 185.5 132.8 8.1 25 A ARG O 138 186.0 132.7 7.0 27 A VAL N 139 184.2 133.1 8.3 26 A VAL CA 139 183.2 133.2 7.2 26 A VAL CB 139 181.8 133.5 7.7 26 A VAL CG1 139 180.9 133.9 6.5 26 A VAL CG2 139 181.3 132.3 8.5 26 A VAL C 139 183.7 134.4 6.3 26 A VAL O 139 183.9 134.2 5.1 25 A LEU N 140 183.9 135.6 6.9 24 A LEU CA 140 184.3 136.7 6.1 25 A LEU CB 140 184.4 137.9 7.0 24 A LEU CG 140 183.0 138.3 7.6 25 A LEU CD1 140 183.1 139.4 8.5 26 A LEU CD2 140 182.1 138.5 6.5 25 A LEU C 140 185.6 136.5 5.4 27 A LEU O 140 185.9 137.0 4.3 28 A LEU N 141 186.5 135.7 6.1 29 A LEU CA 141 187.8 135.3 5.5 30 A LEU CB 141 188.6 134.5 6.5 28 A LEU CG 141 189.4 135.1 7.7 27 A LEU CD1 141 190.1 134.0 8.4 26 A LEU CD2 141 190.5 136.0 7.1 25 A LEU C 141 187.6 134.6 4.2 33 A LEU O 141 188.4 134.8 3.3 34 A ARG N 142 186.6 133.8 4.2 37 A ARG CA 142 186.2 133.0 3.0 41 A ARG CB 142 185.2 131.9 3.3 46 A ARG CG 142 185.6 131.0 4.5 51 A ARG CD 142 184.4 130.2 5.1 55 A ARG NE 142 184.5 130.0 6.5 59 A ARG CZ 142 183.9 129.0 7.3 60 A ARG NH1 142 183.3 128.0 6.7 61 A ARG NH2 142 184.0 129.1 8.6 61 A ARG C 142 185.7 133.9 1.9 41 A ARG O 142 186.2 134.0 0.8 41 A SER N 143 184.6 134.6 2.2 40 A SER CA 143 184.0 135.5 1.3 39 A SER CB 143 182.8 136.2 1.9 39 A SER OG 143 182.0 135.2 2.5 41 A SER C 143 184.8 136.6 0.7 39 A SER O 143 184.9 136.8 −0.5 40 A LEU N 144 185.4 137.5 1.6 38 A LEU CA 144 186.3 138.6 1.1 37 A LEU CB 144 186.5 139.6 2.2 37 A LEU CG 144 185.4 139.9 3.3 36 A LEU CD1 144 185.9 140.9 4.2 37 A LEU CD2 144 184.1 140.3 2.7 36 A LEU C 144 187.6 138.1 0.5 38 A LEU O 144 188.4 138.9 0.1 38 A GLN N 145 187.8 136.8 0.6 38 A GLN CA 145 189.1 136.2 0.1 39 A GLN CB 145 189.1 136.1 −1.4 42 A GLN CG 145 188.2 134.9 −1.9 47 A GLN CD 145 188.3 134.7 −3.4 51 A GLN OE1 145 188.1 135.7 −4.2 52 A GLN NE2 145 188.7 133.5 −3.8 53 A GLN C 145 190.2 137.0 0.6 36 A GLN O 145 191.0 137.6 −0.2 35 A LYS N 146 190.4 137.0 1.9 34 A LYS CA 146 191.4 137.7 2.6 33 A LYS CB 146 191.1 137.9 4.1 33 A LYS CG 146 189.8 138.7 4.3 33 A LYS CD 146 189.8 140.1 3.7 32 A LYS CE 146 190.9 140.9 4.3 33 A LYS NZ 146 190.7 142.3 3.9 33 A LYS C 146 192.7 137.0 2.5 32 A LYS O 146 192.7 135.8 2.3 31 A ASP N 147 193.8 137.8 2.5 32 A ASP CA 147 195.1 137.2 2.5 32 A ASP CB 147 196.2 138.2 2.3 32 A ASP CG 147 197.6 137.7 2.2 33 A ASP OD1 147 198.0 136.9 3.0 34 A ASP OD2 147 198.3 138.0 1.2 35 A ASP C 147 195.3 136.4 3.8 33 A ASP O 147 195.4 137.0 4.9 33 A LEU N 148 195.3 135.1 3.7 33 A LEU CA 148 195.5 134.3 4.9 32 A LEU CB 148 195.1 132.8 4.6 30 A LEU CG 148 193.6 132.6 4.2 29 A LEU CD1 148 193.4 131.1 4.0 28 A LEU CD2 148 192.7 133.1 5.2 28 A LEU C 148 196.9 134.3 5.6 32 A LEU O 148 197.0 134.0 6.7 34 A GLN N 149 197.9 134.7 4.8 33 A GLN CA 149 199.2 134.8 5.4 33 A GLN CB 149 200.3 134.9 4.4 34 A GLN CG 149 201.6 134.3 4.9 36 A GLN CD 149 201.3 133.0 5.6 37 A GLN OE1 149 201.1 131.9 4.9 35 A GLN NE2 149 201.3 133.0 6.9 38 A GLN C 149 199.2 136.1 6.3 34 A GLN O 149 199.9 136.1 7.3 36 A GLU N 150 198.4 137.1 5.9 35 A GLU CA 150 198.4 138.3 6.7 36 A GLU CB 150 197.7 139.4 5.9 40 A GLU CG 150 198.7 140.5 5.4 45 A GLU CD 150 199.9 140.0 4.6 47 A GLU OE1 150 201.0 140.4 4.9 48 A GLU OE2 150 199.6 139.3 3.6 48 A GLU C 150 197.5 138.0 7.9 35 A GLU O 150 197.8 138.5 9.0 36 A GLU N 151 196.6 137.1 7.8 33 A GLU CA 151 195.8 136.6 8.9 31 A GLU CB 151 194.5 135.8 8.4 30 A GLU CG 151 193.6 135.3 9.5 28 A GLU CD 151 192.8 136.4 10.3 29 A GLU OE1 151 192.9 137.6 10.0 28 A GLU OE2 151 192.0 136.0 11.2 29 A GLU C 151 196.6 135.8 9.9 31 A GLU O 151 196.4 135.8 11.1 32 A MET N 152 197.6 135.1 9.4 30 A MET CA 152 198.5 134.3 10.2 29 A MET CB 152 199.5 133.5 9.4 29 A MET CG 152 199.0 132.2 8.9 30 A MET SD 152 199.0 131.0 10.2 31 A MET CE 152 200.6 130.3 9.9 32 A MET C 152 199.2 135.3 11.1 28 A MET O 152 199.4 135.1 12.3 28 A ASN N 153 199.6 136.4 10.5 28 A ASN CA 153 200.3 137.5 11.3 28 A ASN CB 153 200.6 138.6 10.3 29 A ASN CG 153 201.6 138.2 9.2 29 A ASN OD1 153 202.1 137.1 9.2 28 A ASN ND2 153 201.9 139.1 8.3 30 A ASN C 153 199.4 138.0 12.4 28 A ASN O 153 199.9 138.2 13.5 27 A TYR N 154 198.1 138.1 12.1 27 A TYR CA 154 197.2 138.6 13.1 26 A TYR CB 154 195.8 138.7 12.5 25 A TYR CG 154 194.6 138.9 13.4 25 A TYR CD1 154 194.5 140.2 14.1 25 A TYR CE1 154 193.5 140.4 15.0 25 A TYR CD2 154 193.7 137.9 13.7 26 A TYR CE2 154 192.7 138.2 14.6 26 A TYR CZ 154 192.6 139.4 15.3 26 A TYR OH 154 191.6 139.6 16.2 27 A TYR C 154 197.1 137.5 14.2 25 A TYR O 154 197.4 137.8 15.4 26 A ILE N 155 196.7 136.3 13.9 23 A ILE CA 155 196.6 135.3 14.9 21 A ILE CB 155 196.0 134.0 14.3 20 A ILE CG2 155 197.0 133.2 13.6 19 A ILE CG1 155 195.3 133.2 15.4 19 A ILE CD1 155 194.0 133.9 16.0 16 A ILE C 155 197.8 135.0 15.7 21 A ILE O 155 197.8 134.6 16.8 21 A THR N 156 199.0 135.4 15.1 21 A THR CA 156 200.2 135.2 15.8 21 A THR CB 156 201.4 135.4 14.9 21 A THR OG1 156 201.5 134.4 13.9 22 A THR CG2 156 202.8 135.5 15.6 21 A THR C 156 200.3 136.2 17.0 22 A THR O 156 200.6 135.9 18.1 23 A ALA N 157 200.0 137.5 16.6 22 A ALA CA 157 200.0 138.6 17.6 21 A ALA CB 157 199.6 139.8 16.9 19 A ALA C 157 199.0 138.3 18.8 21 A ALA O 157 199.4 138.3 19.9 22 A ILE N 158 197.8 138.0 18.4 21 A ILE CA 158 196.7 137.7 19.4 22 A ILE CB 158 195.4 137.4 18.7 21 A ILE CG2 158 194.3 137.0 19.7 22 A ILE CG1 158 194.9 138.7 18.0 23 A ILE CD1 158 194.7 139.8 19.0 25 A ILE C 158 197.0 136.5 20.3 22 A ILE O 158 196.7 136.6 21.5 23 A ILE N 159 197.6 135.5 19.8 22 A ILE CA 159 197.9 134.3 20.6 21 A ILE CB 159 198.4 133.1 19.8 19 A ILE CG2 159 198.9 132.0 20.8 18 A ILE CG1 159 197.3 132.5 19.0 18 A ILE CD1 159 197.9 131.6 17.9 18 A ILE C 159 199.1 134.8 21.6 23 A ILE O 159 199.0 134.4 22.8 24 A GLU N 160 200.0 135.5 21.1 24 A GLU CA 160 201.1 136.0 21.9 25 A GLU CB 160 202.1 136.8 21.2 24 A GLU CG 160 202.9 136.1 20.1 23 A GLU CD 160 204.1 135.4 20.5 23 A GLU OE1 160 204.5 135.4 21.7 23 A GLU OE2 160 204.7 134.7 19.7 23 A GLU C 160 200.5 136.7 23.1 27 A GLU O 160 201.0 136.6 24.2 28 A GLU N 161 199.5 137.6 22.9 28 A GLU CA 161 199.0 138.3 24.0 31 A GLU CB 161 198.4 139.6 23.6 32 A GLU CG 161 197.2 139.5 22.7 37 A GLU CD 161 197.1 140.7 21.8 39 A GLU OE1 161 198.2 141.1 21.2 41 A GLU OE2 161 196.0 141.3 21.6 41 A GLU C 161 198.0 137.5 24.9 31 A GLU O 161 197.9 137.7 26.1 33 A GLN N 162 197.4 136.4 24.4 30 A GLN CA 162 196.5 135.5 25.1 28 A GLN CB 162 195.1 136.1 25.2 32 A GLN CG 162 194.5 136.7 23.9 35 A GLN CD 162 193.3 137.6 24.3 39 A GLN OE1 162 192.5 137.2 25.1 39 A GLN NE2 162 193.2 138.7 23.6 40 A GLN C 162 196.6 134.1 24.6 26 A GLN O 162 195.6 133.6 24.0 25 A PRO N 163 197.6 133.4 25.0 23 A PRO CD 163 198.7 133.8 25.9 21 A PRO CA 163 197.9 132.0 24.5 22 A PRO CB 163 199.4 131.8 24.8 20 A PRO CG 163 199.6 132.5 26.0 20 A PRO C 163 197.1 130.9 25.3 22 A PRO O 163 197.3 129.7 25.1 23 A LYS N 164 196.2 131.4 26.2 22 A LYS CA 164 195.4 130.5 27.0 21 A LYS CB 164 195.6 130.6 28.5 20 A LYS CG 164 196.9 130.0 29.0 21 A LYS CD 164 197.0 129.9 30.4 19 A LYS CE 164 198.3 129.5 30.8 20 A LYS NZ 164 198.4 129.3 32.3 21 A LYS C 164 194.0 130.8 26.6 21 A LYS O 164 193.3 131.4 27.4 22 A ASN N 165 193.6 130.4 25.4 21 A ASN CA 165 192.3 130.6 24.9 20 A ASN CB 165 192.2 132.0 24.2 21 A ASN CG 165 191.0 132.1 23.3 21 A ASN OD1 165 190.8 131.4 22.4 23 A ASN ND2 165 190.1 133.1 23.6 22 A ASN C 165 192.2 129.5 23.8 19 A ASN O 165 193.1 129.1 23.2 20 A TYR N 166 191.0 128.9 23.8 19 A TYR CA 166 190.7 127.8 22.9 18 A TYR CB 166 189.5 127.0 23.3 19 A TYR CG 166 189.8 126.0 24.4 20 A TYR CD1 166 189.4 126.4 25.7 21 A TYR CE1 166 189.5 125.5 26.8 22 A TYR CD2 166 190.3 124.8 24.2 22 A TYR CE2 166 190.5 123.9 25.3 22 A TYR CZ 166 190.1 124.2 26.6 22 A TYR OH 166 190.3 123.4 27.6 23 A TYR C 166 190.5 128.2 21.4 18 A TYR O 166 190.9 127.5 20.5 18 A GLN N 167 189.8 129.4 21.2 17 A GLN CA 167 189.5 129.9 19.9 17 A GLN CB 167 188.5 131.0 20.0 17 A GLN CG 167 187.1 130.6 20.4 18 A GLN CD 167 187.1 130.1 21.8 20 A GLN OE1 167 187.8 130.7 22.7 22 A GLN NE2 167 186.3 129.1 22.1 22 A GLN C 167 190.7 130.4 19.1 16 A GLN O 167 190.8 130.1 17.9 18 A VAL N 168 191.7 131.0 19.7 16 A VAL CA 168 192.8 131.5 19.0 15 A VAL CB 168 193.7 132.5 19.9 14 A VAL CG1 168 192.9 133.7 20.4 14 A VAL CG2 168 194.3 131.8 21.1 14 A VAL C 168 193.6 130.4 18.4 17 A VAL O 168 193.8 130.4 17.2 19 A TRP N 169 194.0 129.4 19.2 17 A TRP CA 169 194.7 128.3 18.7 16 A TRP CB 169 195.1 127.3 19.8 14 A TRP CG 169 196.2 127.9 20.7 14 A TRP CD2 169 197.6 127.9 20.4 13 A TRP CE2 169 198.2 128.5 21.5 13 A TRP CE3 169 198.3 127.4 19.3 12 A TRP CD1 169 196.0 128.5 21.9 13 A TRP NE1 169 197.2 128.9 22.4 14 A TRP CZ2 169 199.6 128.6 21.6 13 A TRP CZ3 169 199.7 127.5 19.4 13 A TRP CH2 169 200.4 128.1 20.5 13 A TRP C 169 194.0 127.5 17.6 17 A TRP O 169 194.5 127.2 16.6 17 A HIS N 170 192.7 127.3 17.8 19 A HIS CA 170 191.9 126.6 16.8 20 A HIS CB 170 190.5 126.3 17.3 22 A HIS CG 170 189.6 125.6 16.3 24 A HIS CD2 170 188.6 126.0 15.5 26 A HIS ND1 170 189.9 124.3 15.9 25 A HIS CE1 170 189.1 123.9 15.0 26 A HIS NE2 170 188.3 124.9 14.7 26 A HIS C 170 191.8 127.4 15.5 20 A HIS O 170 191.7 126.8 14.4 22 A HIS N 171 191.7 128.7 15.6 20 A HIS CA 171 191.7 129.5 14.5 18 A HIS CB 171 191.4 131.0 14.9 18 A HIS CG 171 191.3 131.9 13.7 17 A HIS CD2 171 192.2 132.7 13.1 17 A HIS ND1 171 190.1 132.2 13.1 16 A HIS CE1 171 190.3 133.1 12.2 16 A HIS NE2 171 191.5 133.4 12.2 17 A HIS C 171 193.0 129.4 13.8 18 A HIS O 171 193.1 129.3 12.5 19 A ARG N 172 194.1 129.3 14.5 18 A ARG CA 172 195.4 129.1 13.9 18 A ARG CB 172 196.5 129.2 14.9 17 A ARG CG 172 197.9 129.3 14.2 17 A ARG CD 172 199.0 129.4 15.2 17 A ARG NE 172 200.3 129.4 14.5 18 A ARG CZ 172 200.9 130.5 14.2 19 A ARG NH1 172 200.5 131.7 14.5 18 A ARG NH2 172 202.1 130.4 13.6 19 A ARG C 172 195.5 127.9 13.1 20 A ARG O 172 196.1 127.8 12.1 22 A ARG N 173 194.9 126.8 13.6 21 A ARG CA 173 194.9 125.5 13.0 21 A ARG CB 173 194.3 124.5 14.0 21 A ARG CG 173 194.1 123.1 13.4 23 A ARG CD 173 193.4 122.2 14.3 26 A ARG NE 173 192.9 121.0 13.7 29 A ARG CZ 173 192.9 119.8 14.1 31 A ARG NH1 173 193.5 119.5 15.3 32 A ARG NH2 173 192.4 118.8 13.4 32 A ARG C 173 194.1 125.5 11.8 22 A ARG O 173 194.4 124.8 10.8 23 A VAL N 174 192.9 126.2 11.8 24 A VAL CA 174 192.1 126.3 10.6 25 A VAL CB 174 190.8 127.0 10.9 25 A VAL CG1 174 190.1 127.2 9.6 25 A VAL CG2 174 190.0 126.2 11.8 24 A VAL C 174 192.9 126.9 9.4 27 A VAL O 174 192.8 126.4 8.3 29 A LEU N 175 193.6 128.0 9.7 27 A LEU CA 175 194.4 128.7 8.7 27 A LEU CB 175 195.1 129.9 9.3 26 A LEU CG 175 194.2 131.0 9.9 27 A LEU CD1 175 195.1 132.2 10.4 26 A LEU CD2 175 193.2 131.5 8.8 26 A LEU C 175 195.5 127.8 8.1 28 A LEU O 175 195.7 127.7 6.9 30 A VAL N 176 196.2 127.1 9.0 29 A VAL CA 176 197.3 126.2 8.6 28 A VAL CB 176 198.1 125.6 9.8 28 A VAL CG1 176 199.1 124.5 9.3 27 A VAL CG2 176 198.8 126.7 10.5 28 A VAL C 176 196.7 125.0 7.7 28 A VAL O 176 197.4 124.5 6.8 28 A GLU N 177 195.4 124.7 8.0 28 A GLU CA 177 194.8 123.7 7.2 29 A GLU CB 177 193.5 123.2 7.9 30 A GLU CG 177 193.8 122.3 9.1 32 A GLU CD 177 192.6 121.8 9.8 34 A GLU OE1 177 192.6 120.7 10.4 34 A GLU OE2 177 191.6 122.5 9.7 35 A GLU C 177 194.5 124.2 5.8 29 A GLU O 177 194.8 123.6 4.8 29 A TRP N 178 193.8 125.4 5.8 28 A TRP CA 178 193.4 126.0 4.5 26 A TRP CB 178 192.9 127.4 4.8 24 A TRP CG 178 191.4 127.4 5.2 22 A TRP CD2 178 190.6 128.5 5.6 21 A TRP CE2 178 189.3 128.0 6.0 20 A TRP CE3 178 190.9 129.8 6.1 22 A TRP CD1 178 190.5 126.3 5.1 22 A TRP NE1 178 189.3 126.7 5.6 21 A TRP CZ2 178 188.3 128.8 6.5 20 A TRP CZ3 178 189.9 130.6 6.7 21 A TRP CH2 178 188.6 130.1 6.8 20 A TRP C 178 194.7 126.2 3.7 28 A TRP O 178 194.7 125.9 2.5 29 A LEU N 179 195.7 126.7 4.3 28 A LEU CA 179 197.0 127.0 3.6 30 A LEU CB 179 197.8 128.0 4.4 30 A LEU CG 179 197.4 129.5 4.6 30 A LEU CD1 179 198.4 130.2 5.4 30 A LEU CD2 179 197.3 130.1 3.2 30 A LEU C 179 197.9 125.8 3.4 32 A LEU O 179 198.8 125.8 2.7 32 A LYS N 180 197.6 124.7 4.2 34 A LYS CA 180 198.5 123.5 4.1 35 A LYS CB 180 198.3 122.9 2.7 36 A LYS CG 180 196.8 122.6 2.5 39 A LYS CD 180 196.5 122.6 1.0 42 A LYS CE 180 195.1 122.1 0.8 44 A LYS NZ 180 194.8 120.7 1.4 44 A LYS C 180 199.9 124.0 4.3 35 A LYS O 180 200.8 123.4 3.7 36 A ASP N 181 200.1 125.0 5.1 34 A ASP CA 181 201.5 125.5 5.4 33 A ASP CB 181 201.5 127.0 4.9 32 A ASP CG 181 202.9 127.5 4.8 32 A ASP OD1 181 203.9 126.8 5.2 31 A ASP OD2 181 203.1 128.7 4.5 33 A ASP C 181 201.9 125.5 6.9 34 A ASP O 181 201.4 126.3 7.7 34 A PRO N 182 202.7 124.5 7.2 33 A PRO CD 182 203.0 123.2 6.5 32 A PRO CA 182 203.2 124.3 8.6 32 A PRO CB 182 203.3 122.8 8.8 32 A PRO CG 182 203.8 122.4 7.4 31 A PRO C 182 204.6 124.9 8.8 32 A PRO O 182 205.1 124.8 9.9 33 A SER N 183 205.2 125.5 7.8 32 A SER CA 183 206.5 126.1 7.9 33 A SER CB 183 206.9 126.8 6.6 34 A SER OG 183 206.1 127.9 6.5 37 A SER C 183 206.8 127.0 9.1 33 A SER O 183 207.9 126.9 9.7 35 A GLN N 184 205.8 127.8 9.5 32 A GLN CA 184 206.1 128.7 10.7 32 A GLN CB 184 205.6 130.1 10.4 33 A GLN CG 184 204.4 130.2 9.5 34 A GLN CD 184 204.0 131.7 9.3 34 A GLN OE1 184 204.2 132.5 10.2 34 A GLN NE2 184 203.3 131.9 8.2 35 A GLN C 184 205.7 128.2 12.1 30 A GLN O 184 206.0 128.8 13.1 29 A GLU N 185 205.1 127.0 12.1 27 A GLU CA 185 204.6 126.5 13.4 25 A GLU CB 185 203.6 125.3 13.1 25 A GLU CG 185 202.4 125.6 12.2 25 A GLU CD 185 201.7 126.9 12.5 25 A GLU OE1 185 200.8 126.9 13.3 25 A GLU OE2 185 202.1 127.9 11.9 27 A GLU C 185 205.5 126.1 14.5 24 A GLU O 185 205.4 126.6 15.6 24 A LEU N 186 206.4 125.1 14.2 23 A LEU CA 186 207.3 124.7 15.3 23 A LEU CB 186 208.3 123.6 14.8 21 A LEU CG 186 207.6 122.3 14.4 20 A LEU CD1 186 208.6 121.2 14.2 20 A LEU CD2 186 206.6 121.9 15.4 18 A LEU C 186 208.1 125.9 15.9 24 A LEU O 186 208.4 125.9 17.1 26 A GLU N 187 208.3 126.9 15.1 26 A GLU CA 187 209.0 128.1 15.6 28 A GLU CB 187 209.6 128.9 14.4 31 A GLU CG 187 210.5 130.0 14.8 35 A GLU CD 187 211.0 130.8 13.6 37 A GLU OE1 187 211.2 130.1 12.5 38 A GLU OE2 187 211.2 132.0 13.7 39 A GLU C 187 208.1 129.1 16.4 27 A GLU O 187 208.6 129.6 17.4 27 A PHE N 188 206.9 129.3 16.0 25 A PHE CA 188 205.9 130.1 16.7 23 A PHE CB 188 204.7 130.3 15.9 23 A PHE CG 188 203.5 130.8 16.7 23 A PHE CD1 188 203.5 132.0 17.2 23 A PHE CD2 188 202.5 129.9 17.0 23 A PHE CE1 188 202.5 132.5 18.0 23 A PHE CE2 188 201.4 130.4 17.8 24 A PHE CZ 188 201.4 131.7 18.3 23 A PHE C 188 205.6 129.5 18.0 23 A PHE O 188 205.6 130.1 19.1 23 A ILE N 189 205.3 128.2 18.0 23 A ILE CA 189 205.0 127.4 19.2 24 A ILE CB 189 204.7 125.9 18.9 22 A ILE CG2 189 204.3 125.1 20.1 22 A ILE CG1 189 203.6 125.8 17.8 21 A ILE CD1 189 203.3 124.5 17.3 20 A ILE C 189 206.2 127.5 20.2 24 A ILE O 189 205.9 127.7 21.4 24 A ALA N 190 207.4 127.3 19.7 25 A ALA CA 190 208.6 127.4 20.6 24 A ALA CB 190 209.8 127.0 19.8 23 A ALA C 190 208.7 128.8 21.2 25 A ALA O 190 209.4 128.9 22.3 26 A ASP N 191 208.2 129.8 20.6 26 A ASP CA 191 208.3 131.1 21.2 26 A ASP CB 191 208.0 132.2 20.2 28 A ASP CG 191 208.1 133.6 20.8 30 A ASP OD1 191 209.2 133.9 21.4 31 A ASP OD2 191 207.1 134.4 20.8 31 A ASP C 191 207.2 131.2 22.3 25 A ASP O 191 207.5 131.9 23.3 27 A ILE N 192 206.0 130.7 22.1 23 A ILE CA 192 205.0 130.7 23.2 21 A ILE CB 192 203.7 130.1 22.7 20 A ILE CG2 192 202.7 130.0 23.8 19 A ILE CG1 192 203.2 130.9 21.5 18 A ILE CD1 192 202.8 132.2 21.9 17 A ILE C 192 205.5 129.8 24.4 22 A ILE O 192 205.4 130.3 25.5 22 A LEU N 193 206.1 128.7 24.1 23 A LEU CA 193 206.7 127.8 25.1 23 A LEU CB 193 207.1 126.4 24.6 21 A LEU CG 193 205.9 125.6 24.0 21 A LEU CD1 193 206.5 124.3 23.5 21 A LEU CD2 193 204.9 125.3 25.1 20 A LEU C 193 207.9 128.4 25.8 25 A LEU O 193 208.4 127.9 26.8 26 A ASN N 194 208.4 129.4 25.2 25 A ASN CA 194 209.5 130.0 25.8 26 A ASN CB 194 210.4 130.7 24.7 29 A ASN CG 194 211.5 131.5 25.3 30 A ASN OD1 194 211.5 132.7 25.3 33 A ASN ND2 194 212.5 130.8 25.9 30 A ASN C 194 209.0 131.0 26.8 27 A ASN O 194 209.7 131.4 27.8 29 A GLN N 195 207.7 131.3 26.7 26 A GLN CA 195 207.1 132.3 27.6 25 A GLN CB 195 206.1 133.1 26.9 26 A GLN CG 195 206.8 134.1 25.9 27 A GLN CD 195 205.9 134.6 24.7 27 A GLN OE1 195 205.0 135.3 24.9 28 A GLN NE2 195 206.3 134.2 23.5 27 A GLN C 195 206.4 131.5 28.8 24 A GLN O 195 206.6 131.8 29.9 25 A ASP N 196 205.7 130.4 28.4 22 A ASP CA 196 205.0 129.5 29.4 19 A ASP CB 196 203.6 129.8 29.4 18 A ASP CG 196 202.8 128.8 30.3 17 A ASP OD1 196 203.4 127.8 30.8 17 A ASP OD2 196 201.6 129.0 30.5 17 A ASP C 196 205.3 128.1 28.8 19 A ASP O 196 204.6 127.6 27.9 21 A ALA N 197 206.3 127.5 29.4 18 A ALA CA 197 206.7 126.1 28.9 17 A ALA CB 197 208.0 125.8 29.5 17 A ALA C 197 205.8 125.0 29.1 18 A ALA O 197 206.0 123.9 28.7 19 A LYS N 198 204.6 125.3 29.6 18 A LYS CA 198 203.6 124.2 29.9 18 A LYS CB 198 203.6 123.9 31.4 19 A LYS CG 198 204.9 123.7 32.0 19 A LYS CD 198 204.8 123.1 33.4 20 A LYS CE 198 206.1 122.9 34.1 20 A LYS NZ 198 206.0 122.4 35.5 20 A LYS C 198 202.3 124.5 29.3 18 A LYS O 198 201.3 123.9 29.7 20 A ASN N 199 202.2 125.5 28.5 18 A ASN CA 199 200.9 125.9 27.9 17 A ASN CB 199 201.1 127.0 26.8 17 A ASN CG 199 199.8 127.6 26.4 18 A ASN OD1 199 199.1 127.1 25.6 20 A ASN ND2 199 199.6 128.9 26.9 18 A ASN C 199 200.3 124.7 27.3 18 A ASN O 199 200.9 124.1 26.4 20 A TYR N 200 199.2 124.3 27.8 18 A TYR CA 200 198.5 123.0 27.3 16 A TYR CB 200 197.3 122.7 28.1 17 A TYR CG 200 196.9 121.3 28.1 18 A TYR CD1 200 197.4 120.3 29.0 18 A TYR CE1 200 197.0 119.0 28.9 18 A TYR CD2 200 196.0 120.8 27.1 17 A TYR CE2 200 195.7 119.5 27.0 18 A TYR CZ 200 196.2 118.6 27.8 17 A TYR OH 200 195.8 117.3 27.7 16 A TYR C 200 198.2 123.1 25.8 16 A TYR O 200 198.4 122.2 25.0 16 A HIS N 201 197.6 124.3 25.3 16 A HIS CA 201 197.2 124.5 24.0 16 A HIS CB 201 196.6 125.8 23.8 16 A HIS CG 201 195.5 126.1 24.9 16 A HIS CD2 201 195.6 126.6 26.1 15 A HIS ND1 201 194.2 125.6 24.7 15 A HIS CE1 201 193.5 125.9 25.8 15 A HIS NE2 201 194.3 126.5 26.7 15 A HIS C 201 198.4 124.4 23.0 17 A HIS O 201 198.4 123.8 21.9 17 A ALA N 202 199.5 125.1 23.4 18 A ALA CA 202 200.7 125.1 22.6 18 A ALA CB 202 201.8 126.0 23.4 18 A ALA C 202 201.3 123.8 22.4 19 A ALA O 202 201.8 123.5 21.3 22 A TRP N 203 201.4 122.9 23.4 18 A TRP CA 203 201.9 121.6 23.2 18 A TRP CB 203 202.1 120.9 24.6 18 A TRP CG 203 203.3 121.4 25.3 15 A TRP CD2 203 204.6 121.1 25.0 15 A TRP CE2 203 205.5 121.7 25.9 14 A TRP CE3 203 205.2 120.4 23.9 15 A TRP CD1 203 203.3 122.2 26.4 15 A TRP NE1 203 204.6 122.4 26.8 14 A TRP CZ2 203 206.8 121.7 25.9 14 A TRP CZ3 203 206.6 120.3 23.9 14 A TRP CH2 203 207.4 120.9 24.8 14 A TRP C 203 200.9 120.8 22.4 19 A TRP O 203 201.3 119.9 21.6 20 A GLN N 204 199.6 121.0 22.6 19 A GLN CA 204 198.6 120.3 21.8 19 A GLN CB 204 197.2 120.6 22.3 20 A GLN CG 204 196.2 119.5 21.9 23 A GLN CD 204 194.8 119.8 22.3 23 A GLN OE1 204 193.9 119.7 21.5 25 A GLN NE2 204 194.6 120.1 23.6 24 A GLN C 204 198.7 120.6 20.3 20 A GLN O 204 198.4 119.8 19.5 19 A HIS N 205 198.9 121.9 20.1 20 A HIS CA 205 199.0 122.4 18.7 19 A HIS CB 205 199.1 123.9 18.7 18 A HIS CG 205 199.0 124.5 17.3 18 A HIS CD2 205 199.8 125.2 16.5 18 A HIS ND1 205 197.8 124.4 16.5 18 A HIS CE1 205 198.0 125.0 15.4 17 A HIS NE2 205 199.2 125.5 15.3 17 A HIS C 205 200.3 121.8 18.1 19 A HIS O 205 200.3 121.3 17.0 22 A ARG N 206 201.3 121.8 18.9 20 A ARG CA 206 202.6 121.3 18.5 18 A ARG CB 206 203.6 121.4 19.6 18 A ARG CG 206 205.0 121.3 19.1 18 A ARG CD 206 206.1 121.7 20.2 17 A ARG NE 206 207.4 121.7 19.6 18 A ARG CZ 206 208.0 122.7 19.1 19 A ARG NH1 206 207.4 123.9 19.0 20 A ARG NH2 206 209.2 122.6 18.5 20 A ARG C 206 202.4 119.8 18.1 20 A ARG O 206 202.9 119.5 17.0 22 A GLN N 207 201.8 119.0 18.9 19 A GLN CA 207 201.7 117.6 18.6 19 A GLN CB 207 201.0 116.8 19.7 19 A GLN CG 207 201.7 116.8 21.0 20 A GLN CD 207 201.2 1157 22.0 21 A GLN OE1 207 200.1 115.3 21.9 20 A GLN NE2 207 202.1 115.3 22.8 19 A GLN C 207 200.9 117.3 17.3 21 A GLN O 207 201.1 116.4 16.5 22 A TRP N 208 199.9 118.2 17.0 21 A TRP CA 208 199.1 118.1 15.8 22 A TRP CB 208 197.8 119.0 16.0 20 A TRP CG 208 197.0 119.1 14.7 19 A TRP CD2 208 197.1 120.2 13.7 20 A TRP CE2 208 196.3 119.9 12.7 19 A TRP CE3 208 197.9 121.4 13.7 20 A TRP CD1 208 196.2 118.2 14.2 19 A TRP NE1 208 195.7 118.7 12.9 19 A TRP CZ2 208 196.2 120.7 11.6 18 A TRP CZ3 208 197.7 122.2 12.6 19 A TRP CH2 208 196.9 121.8 11.5 19 A TRP C 208 199.8 118.4 14.5 24 A TRP O 208 199.5 117.8 13.5 26 A VAL N 209 200.6 119.5 14.5 25 A VAL CA 209 201.4 119.9 13.4 25 A VAL CB 209 202.1 121.2 13.6 24 A VAL CG1 209 202.8 121.7 12.3 24 A VAL CG2 209 201.1 122.3 14.0 24 A VAL C 209 202.4 118.8 13.1 26 A VAL O 209 202.6 118.5 11.9 28 A ILE N 210 203.1 118.3 14.1 26 A ILE CA 210 204.1 117.3 13.9 26 A ILE CB 210 204.8 116.9 15.3 25 A ILE CG2 210 205.6 115.7 15.1 24 A ILE CG1 210 205.6 118.1 15.8 23 A ILE CD1 210 206.4 117.7 16.9 24 A ILE C 210 203.5 116.0 13.4 27 A ILE O 210 203.9 115.5 12.4 28 A GLN N 211 202.4 115.6 14.0 30 A GLN CA 211 201.7 114.4 13.5 32 A GLN CB 211 200.6 114.0 14.5 35 A GLN CG 211 200.0 112.7 14.2 39 A GLN CD 211 199.6 111.9 15.5 40 A GLN OE1 211 199.1 112.5 16.5 42 A GLN NE2 211 199.8 110.6 15.5 41 A GLN C 211 201.1 114.6 12.1 33 A GLN O 211 201.2 113.7 11.3 33 A GLU N 212 200.4 115.7 11.9 34 A GLU CA 212 199.8 115.9 10.6 35 A GLU CB 212 198.9 117.2 10.6 37 A GLU CG 212 197.6 117.0 11.2 42 A GLU CD 212 196.8 115.8 10.6 45 A GLU OE1 212 196.2 116.0 9.5 48 A GLU OE2 212 196.8 114.7 11.2 46 A GLU C 212 200.7 116.1 9.4 34 A GLU O 212 200.4 115.5 8.3 35 A PHE N 213 201.8 116.8 9.6 33 A PHE CA 213 202.7 117.1 8.5 32 A PHE CB 213 203.1 118.6 8.5 30 A PHE CG 213 201.9 119.4 8.3 29 A PHE CD1 213 201.0 119.7 9.4 29 A PHE CD2 213 201.5 119.9 7.0 29 A PHE CE1 213 199.9 120.5 9.2 29 A PHE CE2 213 200.4 120.6 6.8 29 A PHE CZ 213 199.6 120.9 7.9 29 A PHE C 213 204.0 116.3 8.6 33 A PHE O 213 205.0 116.6 8.0 35 A ARG N 214 204.0 115.2 9.5 35 A ARG CA 214 205.1 114.4 9.7 36 A ARG CB 214 205.2 113.4 8.5 39 A ARG CG 214 204.3 112.3 8.5 43 A ARG CD 214 203.6 112.1 7.1 46 A ARG NE 214 202.2 112.5 7.2 51 A ARG CZ 214 201.2 111.7 7.6 53 A ARG NH1 214 200.0 112.2 7.7 53 A ARG NH2 214 201.4 110.5 8.0 54 A ARG C 214 206.4 115.1 9.9 36 A ARG O 214 207.4 114.7 9.4 37 A LEU N 215 206.4 116.1 10.8 35 A LEU CA 215 207.6 116.9 11.2 34 A LEU CB 215 207.2 118.3 11.4 34 A LEU CG 215 206.5 119.1 10.3 33 A LEU CD1 215 206.3 120.6 10.7 34 A LEU CD2 215 207.3 119.1 9.0 33 A LEU C 215 208.3 116.3 12.4 34 A LEU O 215 208.6 117.1 13.3 35 A TRP N 216 208.5 115.0 12.4 35 A TRP CA 216 209.2 114.3 13.6 34 A TRP CB 216 208.9 112.8 13.5 32 A TRP CG 216 207.5 112.5 13.4 30 A TRP CD2 216 206.6 112.4 14.5 29 A TRP CE2 216 205.3 112.0 14.0 29 A TRP CE3 216 206.7 112.6 15.9 28 A TRP CD1 216 206.8 112.1 12.3 30 A TRP NE1 216 205.5 111.9 12.6 29 A TRP CZ2 216 204.2 111.9 14.8 29 A TRP CZ3 216 205.6 112.4 16.7 28 A TRP CH2 216 204.3 112.1 16.1 28 A TRP C 216 210.7 114.5 13.8 36 A TRP O 216 211.1 114.5 15.0 38 A ASP N 217 211.4 114.8 12.7 38 A ASP CA 217 212.9 114.8 12.9 39 A ASP CB 217 213.4 115.0 11.5 40 A ASP CG 217 213.0 113.9 10.5 42 A ASP OD1 217 213.1 114.1 9.3 43 A ASP OD2 217 212.6 112.8 11.0 43 A ASP C 217 213.6 115.6 13.9 39 A ASP O 217 214.6 115.1 14.5 39 A ASN N 218 213.2 116.8 14.3 39 A ASN CA 218 213.9 117.6 15.3 38 A ASN CB 218 214.3 118.9 14.7 39 A ASN CG 218 214.9 118.8 13.3 40 A ASN OD1 218 214.2 119.2 12.4 41 A ASN ND2 218 216.1 118.3 13.1 40 A ASN C 218 213.2 117.7 16.6 37 A ASN O 218 213.6 118.5 17.4 38 A GLU N 219 212.1 117.0 16.8 35 A GLU CA 219 211.4 117.1 18.1 34 A GLU CB 219 210.0 116.7 17.9 34 A GLU CG 219 209.1 117.1 19.1 33 A GLU CD 219 209.0 118.6 19.2 33 A GLU OE1 219 209.7 119.4 18.5 33 A GLU OE2 219 208.1 119.0 20.0 34 A GLU C 219 212.1 116.5 19.3 35 A GLU O 219 212.0 117.1 20.4 34 A LEU N 220 212.7 115.3 19.2 35 A LEU CA 220 213.3 114.7 20.3 35 A LEU CB 220 213.8 113.3 20.1 35 A LEU CG 220 214.2 112.4 21.3 35 A LEU CD1 220 213.3 112.5 22.5 35 A LEU CD2 220 214.4 111.0 20.9 34 A LEU C 220 214.5 115.6 20.8 36 A LEU O 220 214.8 115.6 22.0 38 A GLN N 221 215.1 116.3 19.9 37 A GLN CA 221 216.2 117.2 20.2 37 A GLN CB 221 216.9 117.6 18.9 40 A GLN CG 221 217.9 118.6 19.1 45 A GLN CD 221 218.7 118.9 17.8 48 A GLN OE1 221 219.3 118.0 17.2 50 A GLN NE2 221 218.6 120.1 17.2 49 A GLN C 221 215.7 118.4 20.9 36 A GLN O 221 216.4 118.9 21.8 36 A TYR N 222 214.6 118.9 20.6 34 A TYR CA 222 213.9 120.0 21.2 32 A TYR CB 222 212.7 120.4 20.4 30 A TYR CG 222 211.9 121.6 21.0 29 A TYR CD1 222 212.4 122.8 21.0 28 A TYR CE1 222 211.7 123.9 21.5 28 A TYR CD2 222 210.6 121.4 21.5 28 A TYR CE2 222 209.9 122.4 22.0 28 A TYR CZ 222 210.4 123.7 22.0 27 A TYR OH 222 209.7 124.7 22.5 27 A TYR C 222 213.5 119.6 22.6 33 A TYR O 222 213.7 120.4 23.6 33 A VAL N 223 213.0 118.4 22.7 33 A VAL CA 223 212.6 117.8 24.0 32 A VAL CB 223 212.0 116.4 23.8 31 A VAL CG1 223 212.2 115.6 25.1 31 A VAL CG2 223 210.5 116.6 23.5 30 A VAL C 223 213.9 117.8 24.9 33 A VAL O 223 213.8 118.1 26.1 33 A ASP N 224 215.0 117.4 24.4 33 A ASP CA 224 216.2 117.3 25.2 33 A ASP CB 224 217.4 116.7 24.4 33 A ASP CG 224 217.2 115.2 24.2 33 A ASP OD1 224 216.5 114.6 25.0 33 A ASP OD2 224 217.7 114.7 23.2 34 A ASP C 224 216.6 118.7 25.7 34 A ASP O 224 217.2 118.9 26.7 34 A GLN N 225 216.3 119.7 24.8 34 A GLN CA 225 216.6 121.1 25.2 36 A GLN CB 225 216.3 122.0 24.0 38 A GLN CG 225 216.4 123.5 24.3 41 A GLN CD 225 215.8 124.4 23.3 43 A GLN OE1 225 215.8 124.1 22.1 44 A GLN NE2 225 215.3 125.6 23.8 43 A GLN C 225 215.7 121.5 26.4 35 A GLN O 225 216.2 122.0 27.4 35 A LEU N 226 214.4 121.3 26.3 35 A LEU CA 226 213.5 121.8 27.4 34 A LEU CB 226 212.1 121.7 26.9 32 A LEU CG 226 211.8 122.6 25.7 32 A LEU CD1 226 210.3 122.9 25.8 31 A LEU CD2 226 212.5 123.9 25.8 31 A LEU C 226 213.8 121.0 28.7 34 A LEU O 226 213.7 121.6 29.7 34 A LEU N 227 214.1 119.7 28.6 36 A LEU CA 227 214.3 118.9 29.8 36 A LEU CB 227 214.4 117.4 29.5 35 A LEU CG 227 213.1 116.7 29.3 34 A LEU CD1 227 213.3 115.3 28.8 33 A LEU CD2 227 212.4 116.7 30.7 33 A LEU C 227 215.6 119.4 30.5 37 A LEU O 227 215.7 119.4 31.7 38 A LYS N 228 216.5 119.9 29.7 38 A LYS CA 228 217.8 120.4 30.2 39 A LYS CB 228 218.7 120.7 29.0 42 A LYS CG 228 220.1 120.8 29.4 46 A LYS CD 228 221.0 120.6 28.1 49 A LYS CE 228 222.5 120.9 28.4 51 A LYS NZ 228 223.3 120.9 27.1 52 A LYS C 228 217.4 121.7 30.9 39 A LYS O 228 218.0 122.0 32.0 39 A GLU N 229 216.5 122.5 30.4 37 A GLU CA 229 216.1 123.8 31.0 34 A GLU CB 229 215.3 124.6 30.1 34 A GLU CG 229 216.1 125.0 28.8 34 A GLU CD 229 215.3 125.9 27.9 34 A GLU OE1 229 214.1 126.1 28.2 34 A GLU OE2 229 215.8 126.3 26.9 35 A GLU C 229 215.3 123.5 32.3 33 A GLU O 229 215.3 124.2 33.3 33 A ASP N 230 214.5 122.4 32.3 32 A ASP CA 230 213.7 122.0 33.4 30 A ASP CB 230 212.5 123.0 33.5 30 A ASP CG 230 211.7 122.8 34.8 30 A ASP OD1 230 212.1 122.0 35.7 30 A ASP OD2 230 210.8 123.6 35.0 30 A ASP C 230 213.3 120.6 33.4 30 A ASP O 230 212.2 120.3 32.9 29 A VAL N 231 214.1 119.7 33.9 29 A VAL CA 231 213.8 118.3 34.0 29 A VAL CB 231 215.0 117.5 34.7 30 A VAL CG1 231 215.0 117.9 36.2 30 A VAL CG2 231 214.9 116.0 34.4 30 A VAL C 231 212.5 118.0 34.6 28 A VAL O 231 212.0 116.9 34.5 28 A ARG N 232 211.9 118.9 35.3 28 A ARG CA 232 210.6 118.7 36.0 28 A ARG CB 232 210.5 119.5 37.3 29 A ARG CG 232 211.6 119.2 38.3 30 A ARG CD 232 211.3 120.0 39.5 31 A ARG NE 232 212.2 119.7 40.7 32 A ARG CZ 232 213.3 120.3 41.0 32 A ARG NH1 232 213.8 121.3 40.2 32 A ARG NH2 232 214.0 119.9 42.0 33 A ARG C 232 209.4 119.1 35.0 27 A ARG O 232 208.3 119.1 35.5 27 A ASN N 233 209.7 119.4 33.8 26 A ASN CA 233 208.6 119.8 32.9 25 A ASN CB 233 209.1 120.6 31.7 25 A ASN CG 233 207.9 121.3 31.0 25 A ASN OD1 233 206.8 120.9 31.0 26 A ASN ND2 233 208.2 122.5 30.4 24 A ASN C 233 207.9 118.6 32.5 25 A ASN O 233 208.3 117.9 31.5 27 A ASN N 234 206.7 118.3 33.1 25 A ASN CA 234 206.0 117.1 32.7 25 A ASN CB 234 204.8 116.9 33.6 25 A ASN CG 234 204.3 115.5 33.7 25 A ASN OD1 234 205.1 114.6 34.1 25 A ASN ND2 234 203.1 115.2 33.4 25 A ASN C 234 205.6 117.1 31.3 24 A ASN O 234 205.6 116.1 30.6 24 A SER N 235 205.2 118.3 30.8 23 A SER CA 235 204.8 118.5 29.4 21 A SER CB 235 204.5 120.0 29.2 21 A SER OG 235 203.4 120.4 30.0 21 A SER C 235 205.9 118.0 28.4 21 A SER O 235 205.6 117.5 27.3 21 A VAL N 236 207.2 118.2 28.8 22 A VAL CA 236 208.3 117.8 27.9 22 A VAL CB 236 209.5 118.5 28.3 21 A VAL CG1 236 210.6 118.2 27.3 21 A VAL CG2 236 209.3 120.0 28.3 21 A VAL C 236 208.4 116.3 28.1 23 A VAL O 236 208.8 115.6 27.1 25 A TRP N 237 208.2 115.8 29.2 24 A TRP CA 237 208.3 114.3 29.4 25 A TRP CB 237 208.2 113.9 30.8 24 A TRP CG 237 209.5 114.0 31.6 23 A TRP CD2 237 210.6 113.1 31.6 23 A TRP CE2 237 211.6 113.6 32.4 23 A TRP CE3 237 210.8 111.9 31.0 22 A TRP CD1 237 209.8 115.0 32.4 23 A TRP NE1 237 211.1 114.8 32.9 23 A TRP CZ2 237 212.8 113.0 32.7 21 A TRP CZ3 237 212.0 111.2 31.2 21 A TRP CH2 237 213.0 111.8 32.0 21 A TRP C 237 207.2 113.7 28.5 25 A TRP O 237 207.4 112.7 27.8 25 A ASN N 238 206.0 114.3 28.6 24 A ASN CA 238 205.0 113.7 27.7 24 A ASN CB 238 203.7 114.5 28.0 26 A ASN CG 238 202.6 113.9 27.1 28 A ASN OD1 238 202.1 112.8 27.3 29 A ASN ND2 238 202.1 114.8 26.2 27 A ASN C 238 205.3 113.8 26.3 23 A ASN O 238 205.2 112.9 25.6 23 A GLN N 239 205.9 114.9 25.9 24 A GLN CA 239 206.3 115.1 24.5 25 A GLN CB 239 206.9 116.5 24.2 25 A GLN CG 239 207.1 116.8 22.7 25 A GLN CD 239 205.8 117.0 21.9 25 A GLN OE1 239 204.7 116.6 22.4 25 A GLN NE2 239 205.9 117.6 20.8 24 A GLN C 239 207.4 114.0 24.0 25 A GLN O 239 207.3 113.6 22.9 25 A ARG N 240 208.2 113.7 25.0 26 A ARG CA 240 209.3 112.7 24.7 26 A ARG CB 240 210.2 112.6 25.9 27 A ARG CG 240 211.4 111.7 25.7 27 A ARG CD 240 212.2 111.5 27.0 27 A ARG NE 240 213.5 111.0 26.6 28 A ARG CZ 240 214.4 111.7 26.0 29 A ARG NH1 240 214.2 113.0 25.8 30 A ARG NH2 240 215.5 111.2 25.5 29 A ARG C 240 208.7 111.4 24.4 27 A ARG O 240 209.2 110.7 23.5 30 A HIS N 241 207.6 111.0 25.1 27 A HIS CA 241 207.0 109.8 24.9 24 A HIS CB 241 206.1 109.4 26.1 25 A HIS CG 241 205.5 108.1 26.0 25 A HIS CD2 241 205.8 106.9 26.7 25 A HIS ND1 241 204.4 107.7 25.2 24 A HIS CE1 241 204.1 106.5 25.4 25 A HIS NE2 241 204.9 106.0 26.3 25 A HIS C 241 206.1 109.8 23.6 25 A HIS O 241 206.0 108.8 23.0 25 A PHE N 242 205.6 111.0 23.3 24 A PHE CA 242 204.7 111.1 22.1 23 A PHE CB 242 204.2 112.5 22.0 23 A PHE CG 242 203.5 112.9 20.7 22 A PHE CD1 242 202.2 112.3 20.4 22 A PHE CD2 242 204.0 113.8 19.8 22 A PHE CE1 242 201.5 112.7 19.3 21 A PHE CE2 242 203.3 114.1 18.7 22 A PHE CZ 242 202.1 113.6 18.4 22 A PHE C 242 205.6 110.9 20.9 24 A PHE O 242 205.3 110.1 20.0 25 A VAL N 243 206.8 111.5 20.9 25 A VAL CA 243 207.8 111.4 19.8 26 A VAL CB 243 209.0 112.4 20.1 26 A VAL CG1 243 210.1 112.2 19.1 26 A VAL CG2 243 208.4 113.8 20.0 26 A VAL C 243 208.3 110.0 19.6 26 A VAL O 243 208.3 109.5 18.5 27 A ILE N 244 208.9 109.4 20.7 26 A ILE CA 244 209.4 108.1 20.6 25 A ILE CB 244 210.1 107.7 21.9 24 A ILE CG2 244 210.7 106.2 21.8 24 A ILE CG1 244 211.2 108.7 22.2 21 A ILE CD1 244 211.9 108.4 23.5 20 A ILE C 244 208.3 107.1 20.2 25 A ILE O 244 208.5 106.3 19.3 25 A SER N 245 207.2 107.2 20.9 27 A SER CA 245 206.1 106.3 20.5 29 A SER CB 245 204.8 106.8 21.2 29 A SER OG 245 204.8 106.3 22.6 33 A SER C 245 205.7 106.3 19.1 31 A SER O 245 205.5 105.3 18.5 32 A ASN N 246 205.6 107.5 18.5 33 A ASN CA 246 205.2 107.6 17.1 33 A ASN CB 246 204.4 108.9 16.8 33 A ASN CG 246 203.1 108.9 17.6 33 A ASN OD1 246 203.1 109.5 18.7 33 A ASN ND2 246 202.1 108.3 17.1 33 A ASN C 246 206.3 107.4 16.1 34 A ASN O 246 206.1 107.4 14.9 34 A THR N 247 207.6 107.3 16.5 35 A THR CA 247 208.7 107.1 15.6 36 A THR CB 247 209.8 108.2 15.8 35 A THR OG1 247 210.2 108.3 17.2 35 A THR CG2 247 209.2 109.6 15.4 35 A THR C 247 209.2 105.7 15.7 37 A THR O 247 208.8 104.8 15.0 37 A THR N 248 210.1 105.5 16.7 37 A THR CA 248 210.8 104.1 16.8 37 A THR CB 248 212.2 104.3 17.4 37 A THR OG1 248 212.1 104.7 18.8 38 A THR CG2 248 213.0 105.3 16.7 38 A THR C 248 210.0 103.2 17.8 38 A THR O 248 210.0 102.0 17.6 41 A GLY N 249 209.3 103.8 18.8 39 A GLY CA 249 208.6 103.0 19.7 38 A GLY C 249 209.5 102.6 20.8 39 A GLY O 249 210.7 102.9 20.7 38 A TYR N 250 209.0 101.8 21.8 40 A TYR CA 250 209.9 101.3 22.9 42 A TYR CB 250 209.2 101.7 24.2 41 A TYR CG 250 209.2 103.2 24.5 41 A TYR CD1 250 208.2 103.9 23.9 40 A TYR CE1 250 208.0 105.3 24.2 41 A TYR CD2 250 210.1 103.8 25.4 41 A TYR CE2 250 210.0 105.1 25.7 41 A TYR CZ 250 208.9 105.9 25.1 41 A TYR OH 250 208.8 107.2 25.4 41 A TYR C 250 210.2 99.8 22.8 43 A TYR O 250 210.8 99.3 23.7 43 A SER N 251 209.7 99.2 21.7 45 A SER CA 251 209.9 97.7 21.6 47 A SER CB 251 209.2 97.2 20.4 47 A SER OG 251 207.8 97.4 20.6 48 A SER C 251 211.4 97.6 21.3 48 A SER O 251 212.0 96.6 21.9 49 A ASP N 252 212.0 98.5 20.5 49 A ASP CA 252 213.4 98.5 20.2 50 A ASP CB 252 213.7 99.7 19.4 52 A ASP CG 252 215.2 99.8 18.9 53 A ASP OD1 252 216.0 98.8 19.2 55 A ASP OD2 252 215.6 100.8 18.3 54 A ASP C 252 214.2 98.5 21.5 50 A ASP O 252 214.3 99.6 22.2 49 A ARG N 253 214.8 97.4 21.9 49 A ARG CA 253 215.6 97.2 23.1 49 A ARG CB 253 216.3 95.9 23.1 52 A ARG CG 253 215.4 94.7 23.2 55 A ARG CD 253 216.2 93.4 23.1 58 A ARG NE 253 215.4 92.2 23.2 60 A ARG CZ 253 215.7 91.0 22.6 60 A ARG NH1 253 216.7 90.9 21.7 60 A ARG NH2 253 214.9 90.0 22.8 61 A ARG C 253 216.6 98.3 23.3 47 A ARG O 253 217.0 98.6 24.4 46 A ALA N 254 217.2 98.8 22.2 44 A ALA CA 254 218.2 99.8 22.3 42 A ALA CB 254 219.0 99.9 21.0 42 A ALA C 254 217.6 101.1 22.7 41 A ALA O 254 218.2 101.9 23.4 41 A VAL N 255 216.4 101.4 22.2 41 A VAL CA 255 215.7 102.6 22.5 41 A VAL CB 255 214.5 102.9 21.7 41 A VAL CG1 255 213.8 104.2 22.2 41 A VAL CG2 255 214.9 103.1 20.2 41 A VAL C 255 215.3 102.5 24.0 40 A VAL O 255 215.6 103.4 24.8 42 A LEU N 256 214.7 101.4 24.3 40 A LEU CA 256 214.2 101.1 25.7 39 A LEU CB 256 213.7 99.7 25.7 37 A LEU CG 256 213.1 99.2 27.0 37 A LEU CD1 256 212.0 100.1 27.6 37 A LEU CD2 256 212.5 97.8 26.6 37 A LEU C 256 215.4 101.3 26.7 40 A LEU O 256 215.3 102.1 27.6 41 A GLU N 257 216.5 100.7 26.4 42 A GLU CA 257 217.7 100.7 27.3 42 A GLU CB 257 218.8 99.8 26.7 45 A GLU CG 257 220.2 100.1 27.1 48 A GLU CD 257 220.6 99.3 28.4 51 A GLU OE1 257 220.0 99.6 29.5 52 A GLU OE2 257 221.5 98.5 28.3 52 A GLU C 257 218.2 102.2 27.4 42 A GLU O 257 218.5 102.7 28.5 42 A ARG N 258 218.3 102.9 26.3 42 A ARG CA 258 218.7 104.3 26.2 41 A ARG CB 258 218.7 104.8 24.8 40 A ARG CG 258 219.1 106.3 24.6 40 A ARG CD 258 218.6 106.9 23.3 40 A ARG NE 258 217.2 107.2 23.3 40 A ARG CZ 258 216.4 107.2 22.2 40 A ARG NH1 258 216.9 106.8 21.0 41 A ARG NH2 258 215.2 107.4 22.3 40 A ARG C 258 217.8 105.2 27.1 41 A ARG O 258 218.3 106.0 27.8 42 A GLU N 259 216.5 104.9 27.0 41 A GLU CA 259 215.5 105.7 27.7 40 A GLU CB 259 214.1 105.5 27.2 40 A GLU CG 259 213.9 106.1 25.8 40 A GLU CD 259 214.0 107.6 25.8 40 A GLU OE1 259 213.4 108.3 26.7 40 A GLU OE2 259 214.8 108.2 25.0 39 A GLU C 259 215.5 105.3 29.2 40 A GLU O 259 215.4 106.2 30.0 40 A VAL N 260 215.7 104.1 29.5 41 A VAL CA 260 215.7 103.6 30.9 42 A VAL CB 260 215.6 102.1 31.1 41 A VAL CG1 260 215.8 101.7 32.5 41 A VAL CG2 260 214.2 101.7 30.6 41 A VAL C 260 217.0 104.1 31.6 44 A VAL O 260 216.9 104.6 32.7 44 A GLN N 261 218.1 104.1 30.8 45 A GLN CA 261 219.3 104.6 31.4 46 A GLN CB 261 220.5 104.2 30.4 49 A GLN CG 261 221.8 104.0 31.1 52 A GLN CD 261 221.9 102.7 31.8 53 A GLN OE1 261 221.9 101.6 31.2 54 A GLN NE2 261 222.0 102.8 33.2 54 A GLN C 261 219.2 106.1 31.6 45 A GLN O 261 219.5 106.6 32.7 46 A TYR N 262 218.9 106.8 30.5 44 A TYR CA 262 218.7 108.3 30.6 41 A TYR CB 262 218.0 108.8 29.4 41 A TYR CG 262 217.5 110.2 29.6 41 A TYR CD1 262 218.4 111.3 29.6 41 A TYR CE1 262 217.9 112.6 29.8 40 A TYR CD2 262 216.1 110.5 29.7 41 A TYR CE2 262 215.7 111.8 29.9 40 A TYR CZ 262 216.6 112.8 30.0 40 A TYR OH 262 216.2 114.1 30.1 40 A TYR C 262 217.9 108.7 31.8 41 A TYR O 262 218.2 109.6 32.5 41 A THR N 263 216.7 108.1 31.9 41 A THR CA 263 215.7 108.4 32.9 41 A THR CB 263 214.4 107.6 32.7 40 A THR OG1 263 213.9 107.8 31.4 40 A THR CG2 263 213.4 108.0 33.7 40 A THR C 263 216.3 108.1 34.3 41 A THR O 263 216.2 108.9 35.2 41 A LEU N 264 217.0 106.9 34.5 42 A LEU CA 264 217.6 106.6 35.8 43 A LEU CB 264 218.2 105.2 35.7 43 A LEU CG 264 217.3 104.0 35.8 42 A LEU CD1 264 218.2 102.7 35.7 42 A LEU CD2 264 216.5 104.0 37.1 42 A LEU C 264 218.7 107.7 36.1 44 A LEU O 264 218.7 108.1 37.3 43 A GLU N 265 219.4 108.1 35.2 46 A GLU CA 265 220.4 109.2 35.4 48 A GLU CB 265 221.3 109.4 34.2 50 A GLU CG 265 221.6 108.2 33.3 54 A GLU CD 265 222.3 107.1 34.1 57 A GLU OE1 265 221.7 106.0 34.4 58 A GLU OE2 265 223.5 107.2 34.3 58 A GLU C 265 219.7 110.4 35.9 48 A GLU O 265 220.2 111.1 36.8 49 A MET N 266 218.6 110.7 35.3 47 A MET CA 266 217.8 111.9 35.7 46 A MET CB 266 216.6 112.1 34.8 46 A MET CG 266 217.0 112.4 33.3 45 A MET SD 266 218.4 113.5 33.4 44 A MET CE 266 217.7 115.0 32.8 46 A MET C 266 217.3 111.7 37.1 47 A MET O 266 217.2 112.7 37.9 47 A ILE N 267 216.9 110.5 37.4 47 A ILE CA 267 216.4 110.2 38.8 48 A ILE CB 267 215.9 108.7 38.9 47 A ILE CG2 267 215.4 108.4 40.3 46 A ILE CG1 267 214.7 108.5 37.9 46 A ILE CD1 267 214.2 107.1 37.9 46 A ILE C 267 217.5 110.5 39.8 49 A ILE O 267 217.3 111.2 40.7 50 A LYS N 268 218.7 109.9 39.5 50 A LYS CA 268 219.8 110.2 40.3 51 A LYS CB 268 221.1 109.5 39.7 52 A LYS CG 268 221.0 108.0 39.8 54 A LYS CD 268 222.1 107.4 38.9 56 A LYS CE 268 221.6 105.9 38.5 57 A LYS NZ 268 222.5 105.3 37.5 58 A LYS C 268 220.0 111.6 40.6 51 A LYS O 268 220.0 112.0 41.8 52 A LEU N 269 220.1 112.5 39.6 50 A LEU CA 269 220.3 113.9 39.8 49 A LEU CB 269 220.3 114.7 38.5 48 A LEU CG 269 221.2 114.3 37.3 48 A LEU CD1 269 221.2 115.5 36.4 49 A LEU CD2 269 222.6 113.9 37.7 48 A LEU C 269 219.1 114.6 40.6 48 A LEU O 269 219.4 115.4 41.5 49 A VAL N 270 217.9 114.2 40.3 46 A VAL CA 270 216.8 114.8 41.0 44 A VAL CB 270 216.1 115.9 40.1 42 A VAL CG1 270 215.2 116.8 40.9 42 A VAL CG2 270 217.1 116.8 39.5 41 A VAL C 270 215.8 113.8 41.5 44 A VAL O 270 214.7 113.7 41.0 44 A PRO N 271 216.2 113.0 42.5 44 A PRO CD 271 217.4 113.2 43.2 43 A PRO CA 271 215.4 111.9 43.1 43 A PRO CB 271 216.3 111.6 44.4 43 A PRO CG 271 217.6 111.8 43.9 43 A PRO C 271 214.0 112.1 43.5 44 A PRO O 271 213.2 111.2 43.6 44 A HIS N 272 213.7 113.4 43.8 44 A HIS CA 272 212.3 113.7 44.2 44 A HIS CB 272 212.4 114.6 45.4 46 A HIS CG 272 212.8 113.9 46.7 47 A HIS CD2 272 213.9 113.8 47.3 47 A HIS ND1 272 211.8 113.2 47.5 48 A HIS CE1 272 212.4 112.7 48.5 48 A HIS NE2 272 213.7 113.0 48.5 48 A HIS C 272 211.5 114.4 43.1 43 A HIS O 272 210.5 115.1 43.4 43 A ASN N 273 211.9 114.1 41.8 41 A ASN CA 273 211.2 114.6 40.7 39 A ASN CB 273 212.2 115.0 39.5 38 A ASN CG 273 211.5 115.4 38.2 36 A ASN OD1 273 210.3 115.7 38.2 35 A ASN ND2 273 212.2 115.4 37.1 36 A ASN C 273 210.4 113.5 40.2 37 A ASN O 273 210.8 112.5 39.7 37 A GLU N 274 209.1 113.7 40.4 36 A GLU CA 274 208.1 112.7 40.0 35 A GLU CB 274 206.8 113.1 40.5 35 A GLU CG 274 205.7 112.1 40.5 36 A GLU CD 274 204.4 112.6 41.0 38 A GLU OE1 274 203.4 112.2 40.5 39 A GLU OE2 274 204.4 113.4 42.0 39 A GLU C 274 207.9 112.4 38.5 34 A GLU O 274 207.5 111.3 38.2 36 A SER N 275 208.3 113.4 37.7 34 A SER CA 275 208.1 113.2 36.2 33 A SER CB 275 208.3 114.5 35.5 33 A SER OG 275 207.3 115.4 35.9 32 A SER C 275 209.0 112.1 35.7 33 A SER O 275 208.6 111.2 34.9 33 A ALA N 276 210.3 112.1 36.1 33 A ALA CA 276 211.2 111.1 35.6 33 A ALA CB 276 212.6 111.4 36.1 33 A ALA C 276 210.8 109.7 36.2 33 A ALA O 276 211.0 108.7 35.5 32 A TRP N 277 210.1 109.7 37.3 34 A TRP CA 277 209.6 108.5 37.9 33 A TRP CB 277 209.2 108.8 39.4 34 A TRP CG 277 210.4 108.7 40.2 35 A TRP CD2 277 211.1 107.5 40.6 36 A TRP CE2 277 212.1 107.8 41.5 36 A TRP CE3 277 211.0 106.2 40.2 36 A TRP CD1 277 211.0 109.7 40.9 36 A TRP NE1 277 212.0 109.2 41.7 37 A TRP CZ2 277 213.0 106.9 42.0 36 A TRP CZ3 277 211.8 105.2 40.7 35 A TRP CH2 277 212.8 105.6 41.6 36 A TRP C 277 208.3 108.0 37.2 33 A TRP O 277 208.3 106.8 37.0 34 A ASN N 278 207.4 108.8 36.9 32 A ASN CA 278 206.2 108.4 36.2 32 A ASN CB 278 205.2 109.6 36.1 33 A ASN CG 278 204.8 110.0 37.5 33 A ASN OD1 278 205.0 109.3 38.5 33 A ASN ND2 278 204.1 111.1 37.6 34 A ASN C 278 206.6 108.0 34.8 32 A ASN O 278 205.9 107.2 34.2 32 A TYR N 279 207.6 108.5 34.3 30 A TYR CA 279 208.1 108.2 32.9 31 A TYR CB 279 209.1 109.1 32.4 30 A TYR CG 279 209.6 108.9 31.0 30 A TYR CD1 279 208.7 109.2 30.0 31 A TYR CE1 279 209.1 109.0 28.7 31 A TYR CD2 279 210.8 108.4 30.7 31 A TYR CE2 279 211.2 .08.2 29.4 31 A TYR CZ 279 210.4 108.5 28.4 31 A TYR OH 279 210.8 108.3 27.1 32 A TYR C 279 208.7 106.8 33.0 31 A TYR O 279 208.3 105.9 32.1 33 A LEU N 280 209.5 106.5 33.9 32 A LEU CA 280 210.2 105.2 34.1 33 A LEU CB 280 211.0 105.2 35.3 32 A LEU CG 280 211.9 103.9 35.6 32 A LEU CD1 280 212.8 103.6 34.4 30 A LEU CD2 280 212.6 104.0 36.9 30 A LEU C 280 209.1 104.1 34.2 35 A LEU O 280 209.2 103.1 33.5 35 A LYS N 281 208.1 104.4 35.0 37 A LYS CA 281 207.0 103.4 35.2 38 A LYS CB 281 206.1 103.9 36.3 38 A LYS CG 281 205.2 102.8 36.8 38 A LYS CD 281 204.6 103.3 38.2 39 A LYS CE 281 203.8 104.5 38.0 40 A LYS NZ 281 203.5 105.2 39.3 41 A LYS C 281 206.3 103.3 33.9 40 A LYS O 281 206.0 102.2 33.4 41 A GLY N 282 206.0 104.4 33.2 40 A GLY CA 282 205.3 104.4 32.0 40 A GLY C 282 205.9 103.6 30.8 41 A GLY O 282 205.1 103.0 30.1 42 A ILE N 283 207.2 103.6 30.7 42 A ILE CA 283 207.8 102.9 29.6 43 A ILE CB 283 209.1 103.6 29.1 42 A ILE CG2 283 208.8 105.0 28.7 42 A ILE CG1 283 210.2 103.6 30.2 41 A ILE CD1 283 211.5 104.2 29.7 39 A ILE C 283 208.1 101.4 29.8 46 A ILE O 283 208.2 100.6 28.9 47 A LEU N 284 208.2 101.0 31.1 48 A LEU CA 284 208.4 99.6 31.4 49 A LEU CB 284 209.4 99.5 32.6 49 A LEU CG 284 210.8 100.0 32.3 48 A LEU CD1 284 211.7 99.8 33.5 49 A LEU CD2 284 211.4 99.4 31.1 48 A LEU C 284 207.1 98.9 31.9 50 A LEU O 284 207.0 97.7 31.7 49 A GLN N 285 206.2 99.6 32.4 53 A GLN CA 285 204.9 99.1 32.9 56 A GLN CB 285 204.0 100.1 33.6 58 A GLN CG 285 203.4 101.1 32.5 60 A GLN CD 285 202.2 101.8 33.0 62 A GLN OE1 285 201.3 102.1 32.2 62 A GLN NE2 285 202.2 102.2 34.3 62 A GLN C 285 204.1 98.4 31.8 58 A GLN O 285 203.1 97.7 32.1 59 A ASP N 286 204.4 98.8 30.5 60 A ASP CA 286 203.7 98.2 29.5 62 A ASP CB 286 203.3 99.2 28.4 64 A ASP CG 286 201.8 99.6 28.4 66 A ASP OD1 286 201.2 99.8 27.3 67 A ASP OD2 286 201.2 99.7 29.5 67 A ASP C 286 204.3 96.9 28.9 61 A ASP O 286 204.5 96.9 27.6 62 A ARG N 287 204.7 96.0 29.7 60 A ARG CA 287 205.3 94.7 29.4 59 A ARG CB 287 206.7 94.8 28.8 60 A ARG CG 287 207.3 93.5 28.5 61 A ARG CD 287 208.8 93.5 28.2 63 A ARG NE 287 209.4 92.2 28.4 64 A ARG CZ 287 210.3 91.6 27.6 65 A ARG NH1 287 210.6 92.2 26.4 65 A ARG NH2 287 210.7 90.4 27.8 65 A ARG C 287 205.4 94.0 30.7 57 A ARG O 287 205.2 92.7 30.8 58 A GLY N 288 205.6 94.7 31.8 55 A GLY CA 288 205.7 94.1 33.1 53 A GLY C 288 207.0 94.5 33.8 52 A GLY O 288 208.1 94.2 33.3 52 A LEU N 289 206.8 95.2 34.9 51 A LEU CA 289 208.0 95.6 35.7 50 A LEU CB 289 207.6 96.4 36.9 49 A LEU CG 289 207.8 97.9 36.9 47 A LEU CD1 289 207.6 98.5 35.5 47 A LEU CD2 289 206.7 98.5 37.8 47 A LEU C 289 208.8 94.4 36.1 50 A LEU O 289 210.0 94.4 36.3 51 A SER N 290 208.1 93.2 36.3 50 A SER CA 290 208.7 92.0 36.7 51 A SER CB 290 207.7 91.0 37.3 51 A SER OG 290 206.7 90.7 36.3 52 A SER C 290 209.6 91.3 35.7 51 A SER O 290 210.3 90.4 36.0 51 A ARG N 291 209.5 91.8 34.4 51 A ARG CA 291 210.3 91.2 33.3 51 A ARG CB 291 209.5 91.3 32.0 53 A ARG CG 291 208.6 90.2 31.7 56 A ARG CD 291 207.9 90.3 30.4 60 A ARG NE 291 207.6 89.0 29.8 64 A ARG CZ 291 207.6 88.8 28.5 66 A ARG NH1 291 207.3 87.6 28.0 67 A ARG NH2 291 207.8 89.8 27.6 66 A ARG C 291 211.6 91.8 33.2 49 A ARG O 291 212.4 91.6 32.3 48 A TYR N 292 212.0 92.7 34.2 48 A TYR CA 292 213.3 93.3 34.3 46 A TYR CB 292 213.1 94.8 34.1 44 A TYR CG 292 212.4 95.1 32.8 42 A TYR CD1 292 211.0 95.5 32.7 42 A TYR CE1 292 210.4 95.7 31.5 41 A TYR CD2 292 213.1 94.9 31.6 42 A TYR CE2 292 212.4 95.0 30.4 41 A TYR CZ 292 211.1 95.4 30.3 41 A TYR OH 292 210.5 95.6 29.1 40 A TYR C 292 213.8 93.0 35.7 47 A TYR O 292 213.7 93.8 36.7 47 A PRO N 293 214.5 91.9 35.9 47 A PRO CD 293 214.8 90.9 34.8 47 A PRO CA 293 215.0 91.4 37.1 48 A PRO CB 293 215.6 90.0 36.7 47 A PRO CG 293 215.9 90.2 35.3 46 A PRO C 293 216.1 92.3 37.7 49 A PRO O 293 216.2 92.4 38.9 50 A ASN N 294 217.0 92.9 36.9 50 A ASN CA 294 218.0 93.8 37.4 51 A ASN CB 294 219.0 94.2 36.2 50 A ASN CG 294 219.6 93.0 35.5 50 A ASN OD1 294 219.4 92.8 34.3 51 A ASN ND2 294 220.3 92.2 36.3 50 A ASN C 294 217.5 95.1 38.0 52 A ASN O 294 218.0 95.5 39.0 52 A LEU N 295 216.4 95.6 37.4 54 A LEU CA 295 215.8 96.8 37.8 54 A LEU CB 295 214.5 97.0 37.1 54 A LEU CG 295 213.7 98.3 37.2 54 A LEU CD1 295 214.5 99.5 36.7 54 A LEU CD2 295 212.4 98.2 36.5 54 A LEU C 295 215.6 97.0 39.3 55 A LEU O 295 216.0 98.0 39.9 55 A LEU N 296 215.0 95.9 39.9 55 A LEU CA 296 214.8 96.0 41.3 56 A LEU CB 296 214.2 94.6 41.8 55 A LEU CG 296 214.0 94.5 43.3 54 A LEU CD1 296 213.1 95.6 43.8 54 A LEU CD2 296 213.3 93.2 43.6 54 A LEU C 296 216.1 96.2 42.1 58 A LEU O 296 216.1 97.1 43.0 57 A ASN N 297 217.2 95.6 41.7 61 A ASN CA 297 218.5 95.7 42.3 64 A ASN CB 297 219.6 94.9 41.6 66 A ASN CG 297 219.3 93.5 41.4 67 A ASN OD1 297 218.1 93.0 41.5 68 A ASN ND2 297 220.3 92.7 41.0 68 A ASN C 297 218.9 97.2 42.3 64 A ASN O 297 218.8 97.9 43.3 63 A GLN N 298 219.2 97.7 41.1 65 A GLN CA 298 219.6 99.0 40.9 66 A GLN CB 298 219.5 99.4 39.4 66 A GLN CG 298 219.0 98.3 38.4 67 A GLN CD 298 220.2 97.4 38.0 67 A GLN OE1 298 220.6 96.6 38.8 68 A GLN NE2 298 220.6 97.5 36.7 66 A GLN C 298 218.8 100.0 41.7 67 A GLN O 298 219.4 101.0 42.2 68 A LEU N 299 217.5 99.8 41.9 68 A LEU CA 299 216.7 100.7 42.7 69 A LEU CB 299 215.2 100.5 42.4 69 A LEU CG 299 214.5 101.0 41.1 68 A LEU CD1 299 213.0 100.9 41.3 68 A LEU CD2 299 214.8 102.5 40.9 68 A LEU C 299 216.9 100.6 44.2 71 A LEU O 299 217.1 101.5 44.9 70 A LEU N 300 216.9 99.3 44.6 73 A LEU CA 300 217.1 99.0 46.0 74 A LEU CB 300 217.2 97.4 46.1 74 A LEU CG 300 216.1 96.7 46.8 75 A LEU CD1 300 214.7 97.3 46.3 75 A LEU CD2 300 216.1 95.2 46.4 75 A LEU C 300 218.4 99.6 46.5 75 A LEU O 300 218.5 100.1 47.6 76 A ASP N 301 219.4 99.6 45.6 76 A ASP CA 301 220.7 100.2 45.9 78 A ASP CB 301 221.7 99.9 44.8 78 A ASP CG 301 221.9 98.4 44.5 79 A ASP OD1 301 221.4 97.6 45.3 79 A ASP OD2 301 222.6 98.1 43.5 78 A ASP C 301 220.6 101.7 46.2 78 A ASP O 301 221.2 102.2 47.2 79 A LEU N 302 219.8 102.4 45.4 78 A LEU CA 302 219.6 103.9 45.6 79 A LEU CB 302 219.0 104.5 44.4 79 A LEU CG 302 219.9 104.6 43.2 80 A LEU CD1 302 219.2 105.5 42.1 80 A LEU CD2 302 221.2 105.3 43.5 80 A LEU C 302 218.9 104.2 46.9 79 A LEU O 302 218.8 105.4 47.3 78 A GLN N 303 218.3 103.2 47.5 79 A GLN CA 303 217.5 103.3 48.8 80 A GLN CB 303 217.4 102.0 49.5 80 A GLN CG 303 216.1 101.2 49.1 80 A GLN CD 303 214.9 101.8 49.8 80 A GLN OE1 303 214.7 103.0 49.9 80 A GLN NE2 303 214.1 100.9 50.4 80 A GLN C 303 218.1 104.4 49.8 81 A GLN O 303 217.4 105.2 50.3 81 A PRO N 304 219.4 104.3 50.1 81 A PRO CD 304 220.4 103.2 49.9 81 A PRO CA 304 219.9 105.3 51.0 81 A PRO CB 304 221.0 104.5 51.8 81 A PRO CG 304 221.6 103.6 50.6 81 A PRO C 304 220.5 106.5 50.4 81 A PRO O 304 220.4 107.6 51.0 82 A SER N 305 221.2 106.4 49.2 81 A SER CA 305 221.8 107.6 48.6 81 A SER CB 305 223.0 107.2 47.8 81 A SER OG 305 222.7 106.3 46.7 81 A SER C 305 220.9 108.5 47.7 80 A SER O 305 221.1 109.7 47.6 80 A HIS N 306 219.8 107.9 47.1 79 A HIS CA 306 218.9 108.7 46.3 78 A HIS CB 306 219.2 108.4 44.8 79 A HIS CG 306 220.5 108.8 44.4 80 A HIS CD2 306 221.3 108.4 43.3 81 A HIS ND1 306 221.3 109.7 45.0 81 A HIS CE1 306 222.5 109.9 44.4 81 A HIS NE2 306 222.5 109.1 43.4 81 A HIS C 306 217.5 108.3 46.6 77 A HIS O 306 216.7 108.0 45.7 78 A SER N 307 217.1 108.3 47.9 76 A SER CA 307 215.8 108.0 48.3 74 A SER CB 307 215.8 107.6 49.8 74 A SER OG 307 214.6 106.8 50.2 74 A SER C 307 214.7 109.1 48.1 72 A SER O 307 215.0 110.3 48.0 72 A SER N 308 213.4 108.7 48.0 69 A SER CA 308 212.3 109.5 47.8 66 A SER CB 308 212.3 110.2 46.4 66 A SER OG 308 212.2 109.2 45.4 66 A SER C 308 211.1 108.6 47.9 64 A SER O 308 211.2 107.4 47.5 65 A PRO N 309 210.0 109.1 48.4 62 A PRO CD 309 209.6 110.4 48.9 62 A PRO CA 309 208.8 108.1 48.5 60 A PRO CB 309 207.7 109.0 49.1 61 A PRO CG 309 208.1 110.4 48.7 61 A PRO C 309 208.4 107.6 47.1 59 A PRO O 309 207.6 106.7 47.1 60 A TYR N 310 209.1 108.0 46.1 57 A TYR CA 310 208.8 107.6 44.7 54 A TYR CB 310 209.3 108.6 43.7 55 A TYR CG 310 208.8 110.0 44.0 54 A TYR CD1 310 209.7 111.0 44.4 55 A TYR CE1 310 209.2 112.3 44.7 55 A TYR CD2 310 207.4 110.3 43.9 54 A TYR CE2 310 207.0 111.6 44.3 55 A TYR CZ 310 207.9 112.5 44.7 56 A TYR OH 310 207.4 113.8 45.1 57 A TYR C 310 209.5 106.2 44.5 53 A TYR O 310 209.0 105.3 43.9 53 A LEU N 311 210.7 106.1 45.1 50 A LEU CA 311 211.5 104.9 45.0 48 A LEu CB 311 212.8 105.1 45.7 48 A LEU CG 311 213.8 103.9 45.8 48 A LEU CD1 311 214.1 103.3 44.5 48 A LEU CD2 311 215.1 104.4 46.4 48 A LEU C 311 210.7 103.8 45.8 48 A LEU O 311 210.5 102.7 45.3 46 A ILE N 312 210.2 104.2 46.9 47 A ILE CA 312 209.4 103.3 47.8 47 A ILE CB 312 208.9 103.9 49.1 48 A ILE CG2 312 208.2 102.9 50.0 48 A ILE CG1 312 210.1 104.4 49.9 48 A ILE CD1 312 211.1 103.3 50.3 48 A ILE C 312 208.2 102.8 47.0 47 A ILE O 312 207.9 101.6 46.9 49 A ALA N 313 207.4 103.7 46.4 47 A ALA CA 313 206.2 103.3 45.6 45 A ALA CB 313 205.4 104.5 45.2 45 A ALA C 313 206.6 102.5 44.4 43 A ALA O 313 205.8 101.7 43.9 43 A PHE N 314 207.8 102.7 43.8 42 A PHE CA 314 208.2 101.9 42.6 42 A PHE CB 314 209.4 102.5 42.0 42 A PHE CG 314 209.5 102.3 40.5 42 A PHE CD1 314 209.2 103.3 39.6 42 A PHE CD2 314 209.8 101.0 40.0 42 A PHE CE1 314 209.2 103.1 38.2 42 A PHE CE2 314 209.9 100.8 38.6 42 A PHE CZ 314 209.6 101.8 37.7 42 A PHE C 314 208.4 100.4 43.0 41 A PHE O 314 208.0 99.5 42.3 42 A LEU N 315 209.1 100.2 44.1 41 A LEU CA 315 209.4 98.8 44.6 39 A LEU CB 315 210.2 98.8 45.9 39 A LEU CG 315 211.4 99.7 45.9 40 A LEU CD1 315 211.9 99.8 47.3 40 A LEU CD2 315 212.4 99.2 44.9 40 A LEU C 315 208.1 98.1 44.8 38 A LEU O 315 207.9 96.9 44.5 39 A VAL N 316 207.1 98.8 45.4 38 A VAL CA 316 205.8 98.1 45.6 39 A VAL CB 316 204.7 99.0 46.3 39 A VAL CG1 316 203.5 98.3 46.5 39 A VAL CG2 316 205.3 99.5 47.7 39 A VAL C 316 205.2 97.8 44.3 41 A VAL O 316 204.5 96.8 44.1 41 A ASP N 317 205.4 98.7 43.3 43 A ASP CA 317 204.9 98.5 41.9 44 A ASP CB 317 205.1 99.8 41.0 45 A ASP CG 317 204.2 100.9 41.4 46 A ASP OD1 317 203.0 100.6 41.9 46 A ASP OD2 317 204.6 102.1 41.3 46 A ASP C 317 205.6 97.3 41.2 44 A ASP O 317 205.0 96.7 40.3 45 A ILE N 318 206.8 97.0 41.6 44 A ILE CA 318 207.5 95.9 41.0 45 A ILE CB 318 209.0 95.9 41.3 44 A ILE CG2 318 209.7 94.7 40.8 45 A ILE CG1 318 209.6 97.1 40.6 44 A ILE CD1 318 211.1 97.2 40.7 44 A ILE C 318 206.9 94.6 41.7 47 A ILE O 318 206.5 93.7 41.0 47 A TYR N 319 206.8 94.7 43.0 49 A TYR CA 319 206.3 93.5 43.7 51 A TYR CB 319 206.3 93.8 45.2 52 A TYR CG 319 207.7 94.0 45.8 52 A TYR CD1 319 207.9 94.7 47.0 53 A TYR CE1 319 209.2 94.8 47.5 53 A TYR CD2 319 208.8 93.4 45.1 52 A TYR CE2 319 210.1 93.5 45.6 52 A TYR CZ 319 210.3 94.2 46.8 53 A TYR OH 319 211.6 94.3 47.2 54 A TYR C 319 204.9 93.1 43.3 53 A TYR O 319 204.7 92.0 43.1 54 A GLU N 320 204.0 94.1 43.1 55 A GLU CA 320 202.7 93.8 42.6 56 A GLU CB 320 201.9 95.1 42.4 59 A GLU CG 320 201.6 95.9 43.6 62 A GLU CD 320 201.4 97.4 43.3 64 A GLU OE1 320 200.4 98.0 43.9 66 A GLU OE2 320 202.1 98.0 42.5 65 A GLU C 320 202.7 93.0 41.4 56 A GLU O 320 202.0 92.0 41.2 55 A ASP N 321 203.6 93.3 40.5 56 A ASP CA 321 203.7 92.6 39.2 57 A ASP CB 321 204.4 93.4 38.1 56 A ASP CG 321 204.2 92.9 36.8 56 A ASP OD1 321 203.0 92.6 36.4 56 A ASP OD2 321 205.1 92.7 36.0 55 A ASP C 321 204.4 91.3 39.3 58 A ASP O 321 204.1 90.4 38.6 58 A MET N 322 205.4 91.2 40.2 59 A MET CA 322 206.1 89.9 40.3 61 A MET CB 322 207.3 90.0 41.3 60 A MET CG 322 208.5 90.8 40.7 60 A MET SD 322 210.1 90.5 41.5 60 A MET CE 322 209.8 91.2 43.0 59 A MET C 322 205.1 88.8 40.9 63 A MET O 322 205.2 87.7 40.4 63 A LEU N 323 204.3 89.2 41.8 66 A LEU CA 323 203.3 88.3 42.4 69 A LEU CB 323 202.5 89.0 43.5 68 A LEU CG 323 203.0 88.9 45.0 68 A LEU CD1 323 204.4 88.4 45.1 67 A LEU CD2 323 202.8 90.2 45.7 67 A LEU C 323 202.3 87.9 41.3 71 A LEU O 323 202.2 86.7 41.0 72 A GLU N 324 201.8 88.9 40.6 75 A GLU CA 324 200.9 88.7 39.5 78 A GLU CB 324 200.5 90.0 38.8 79 A GLU CG 324 199.6 91.0 39.5 81 A GLU CD 324 199.6 92.4 39.0 82 A GLU OE1 324 199.8 92.7 37.8 82 A GLU OE2 324 199.3 93.3 39.8 82 A GLU C 324 201.5 87.7 38.4 79 A GLU O 324 200.8 86.8 37.9 80 A ASN N 325 202.8 87.8 38.2 80 A ASN CA 325 203.5 86.9 37.2 81 A ASN CB 325 204.4 87.7 36.4 81 A ASN CG 325 203.7 88.8 35.6 82 A ASN OD1 325 204.1 90.0 35.6 82 A ASN ND2 325 202.7 88.4 34.9 82 A ASN C 325 204.1 85.7 37.9 82 A ASN O 325 205.2 85.3 37.4 82 A GLN N 326 203.5 85.2 38.9 84 A GLN CA 326 203.9 84.0 39.6 86 A GLN CB 326 203.5 82.8 38.8 86 A GLN CG 326 202.0 82.8 38.3 87 A GLN CD 326 201.9 83.1 36.8 87 A GLN OE1 326 202.4 82.4 35.9 88 A GLN NE2 326 201.1 84.1 36.5 88 A GLN C 326 205.4 84.0 40.0 86 A GLN O 326 206.1 83.0 39.6 86 A CYS N 327 205.9 85.0 40.7 87 A CYS CA 327 207.3 85.0 41.1 88 A CYS CB 327 207.7 86.4 41.6 87 A CYS SG 327 207.1 86.8 43.3 87 A CYS C 327 207.5 84.0 42.3 90 A CYS O 327 206.5 83.8 43.0 90 A ASP N 328 208.7 83.5 42.4 91 A ASP CA 328 209.0 82.6 43.5 92 A ASP CB 328 210.1 81.6 43.2 93 A ASP CG 328 209.7 80.1 43.4 94 A ASP OD1 328 209.3 79.4 42.5 94 A ASP OD2 328 209.7 79.7 44.6 94 A ASP C 328 209.4 83.4 44.7 92 A ASP O 328 210.1 84.4 44.6 92 A ASN N 329 208.9 83.0 45.9 92 A ASN CA 329 209.0 83.7 47.2 91 A ASN CB 329 210.2 84.7 47.2 91 A ASN CG 329 211.6 83.9 47.1 91 A ASN OD1 329 211.8 83.2 46.2 92 A ASN ND2 329 212.4 84.2 48.2 92 A ASN C 329 207.8 84.5 47.4 91 A ASN O 329 207.8 85.5 48.2 91 A LYS N 330 206.7 84.1 46.8 91 A LYS CA 330 205.4 84.8 47.0 90 A LYS CB 330 204.2 83.9 46.5 91 A LYS CG 330 203.3 84.6 45.5 92 A LYS CD 330 202.2 83.7 45.0 92 A LYS CE 330 201.3 84.3 43.9 92 A LYS NZ 330 202.1 84.6 42.7 91 A LYS C 330 205.1 85.3 48.4 90 A LYS O 330 204.6 86.4 48.6 89 A GLU N 331 205.4 84.5 49.4 89 A GLU CA 331 205.2 84.8 50.8 88 A GLU CB 331 205.6 83.6 51.7 90 A GLU CG 331 204.8 82.3 51.4 92 A GLU CD 331 203.4 82.2 52.1 92 A GLU OE1 331 202.6 81.3 51.7 93 A GLU OE2 331 203.2 83.1 53.0 93 A GLU C 331 206.1 86.0 51.2 87 A GLU O 331 205.6 86.9 51.8 86 A ASP N 332 207.4 85.8 50.9 85 A ASP CA 332 208.4 86.8 51.2 83 A ASP CB 332 209.8 86.2 50.8 84 A ASP CG 332 210.9 87.2 50.8 85 A ASP OD1 332 211.7 87.2 49.8 85 A ASP OD2 332 211.1 88.0 51.7 86 A ASP C 332 208.2 88.2 50.5 82 A ASP O 332 208.1 89.2 51.1 81 A ILE N 333 208.2 88.2 49.1 79 A ILE CA 333 208.0 89.4 48.4 76 A ILE CB 333 208.0 89.1 46.8 76 A ILE CG2 333 207.3 90.1 46.0 75 A ILE CG1 333 209.5 88.9 46.4 75 A ILE CD1 333 209.6 88.3 45.0 75 A ILE C 333 206.7 90.1 48.8 75 A ILE O 333 206.7 91.3 49.0 75 A LEU N 334 205.7 89.4 49.0 74 A LEU CA 334 204.4 89.9 49.5 74 A LEU CB 334 203.4 88.9 49.7 73 A LEU CG 334 202.0 89.3 50.4 73 A LEU CD1 334 201.4 90.4 49.6 73 A LEU CD2 334 201.1 88.1 50.4 73 A LEU C 334 204.6 90.8 50.8 74 A LEU O 334 204.1 91.9 50.8 75 A ASN N 335 205.2 90.2 51.8 74 A ASN CA 335 205.4 90.9 53.0 74 A ASN CB 335 206.2 90.1 54.0 75 A ASN CG 335 205.4 88.9 54.6 76 A ASN OD1 335 204.2 89.1 55.1 76 A ASN ND2 335 205.9 87.7 54.6 76 A ASN C 335 206.1 92.3 52.8 73 A ASN O 335 205.7 93.3 53.5 73 A LYS N 336 207.1 92.3 52.0 72 A LYS CA 336 207.9 93.5 51.7 71 A LYS CB 336 209.0 93.2 50.7 72 A LYS CG 336 210.4 93.2 51.4 72 A LYS CD 336 211.4 92.4 50.5 73 A LYS CE 336 210.9 91.0 50.3 73 A LYS NZ 336 211.8 90.3 49.4 75 A LYS C 336 206.9 94.5 51.1 70 A LYS O 336 206.8 95.6 51.6 70 A ALA N 337 206.2 94.1 50.1 68 A ALA CA 337 205.2 94.9 49.4 66 A ALA CB 337 204.4 94.1 48.4 65 A ALA C 337 204.2 95.5 50.5 65 A ALA O 337 204.0 96.7 50.5 64 A LEU N 338 203.6 94.6 51.3 64 A LEU CA 338 202.6 95.0 52.3 62 A LEU CB 338 202.0 93.8 53.0 62 A LEU CG 338 201.1 92.9 52.1 61 A LEU CD1 338 200.7 91.7 52.9 61 A LEU CD2 338 199.8 93.7 51.8 61 A LEU C 338 203.2 95.9 53.4 62 A LEU O 338 202.6 96.8 53.9 61 A GLU N 339 204.5 95.8 53.7 62 A GLU CA 339 205.2 96.6 54.7 62 A GLU CB 339 206.6 96.0 55.0 65 A GLU CG 339 207.4 96.9 55.9 68 A GLU CD 339 208.9 96.5 56.0 70 A GLU OE1 339 209.2 95.3 56.2 71 A GLU OE2 339 209.7 97.4 55.7 71 A GLU C 339 205.4 98.0 54.1 60 A GLU O 339 205.1 99.0 54.8 60 A LEU N 340 205.9 98.1 52.9 58 A LEU CA 340 206.2 99.3 52.3 55 A LEU CB 340 206.8 99.1 50.9 54 A LEU CG 340 208.1 98.3 50.7 54 A LEU CD1 340 208.7 98.5 49.4 53 A LEU CD2 340 209.0 98.5 51.8 54 A LEU C 340 204.8 100.1 52.2 55 A LEU O 340 204.8 101.3 52.5 55 A CYS N 341 203.8 99.4 51.8 55 A CYS CA 341 202.4 100.0 51.8 55 A CYS CB 341 201.4 99.0 51.4 55 A CYS SG 341 201.5 98.4 49.7 55 A CYS C 341 202.0 100.6 53.1 55 A CYS O 341 201.2 101.6 53.1 55 A GLU N 342 202.5 100.0 54.2 55 A GLU CA 342 202.2 100.5 55.5 54 A GLU CB 342 202.2 99.4 56.6 55 A GLU CG 342 201.4 99.8 57.8 56 A GLU CD 342 199.9 100.3 57.5 57 A GLU OE1 342 199.5 101.3 58.0 57 A GLU OE2 342 199.2 99.6 56.8 58 A GLU C 342 203.1 101.7 55.9 54 A GLU O 342 202.7 102.7 56.5 54 A ILE N 343 204.4 101.5 55.5 54 A ILE CA 343 205.4 102.5 55.8 53 A ILE CB 343 206.8 102.2 55.2 53 A ILE CG2 343 207.7 103.4 55.3 53 A ILE CG1 343 207.4 101.0 55.9 54 A ILE CD1 343 208.9 100.7 55.5 54 A ILE C 343 205.0 103.8 55.1 53 A ILE O 343 205.0 104.9 55.7 53 A LEU N 344 204.6 103.7 53.9 52 A LEU CA 344 204.1 104.8 53.1 51 A LEU CB 344 203.8 104.3 51.7 50 A LEU CG 344 205.0 104.0 50.8 49 A LEU CD1 344 204.6 103.6 49.4 48 A LEU CD2 344 205.9 105.2 50.7 49 A LEU C 344 202.8 105.3 53.8 52 A LEU O 344 202.7 106.5 54.2 53 A ALA N 345 201.8 104.5 53.9 53 A ALA CA 345 200.5 104.9 54.5 55 A ALA CB 345 199.5 103.7 54.5 54 A ALA C 345 200.6 105.5 55.9 56 A ALA O 345 199.6 106.5 56.2 56 A LYS N 346 201.5 105.0 56.8 58 A LYS CA 346 201.6 105.5 58.1 59 A LYS CB 346 202.0 104.4 59.1 61 A LYS CG 346 200.9 103.6 59.8 63 A LYS CD 346 201.5 102.5 60.7 66 A LYS CE 346 200.5 101.5 61.3 67 A LYS NZ 346 201.1 100.5 62.2 67 A LYS C 346 202.7 106.6 58.3 59 A LYS O 346 202.6 107.5 59.1 58 A GLU N 347 203.7 106.5 57.5 59 A GLU CA 347 204.9 107.4 57.6 59 A GLU CB 347 206.0 106.6 58.1 61 A GLU CG 347 207.3 107.4 58.2 63 A GLU CD 347 208.6 106.5 58.4 65 A GLU OE1 347 209.7 107.0 58.6 66 A GLU OE2 347 208.4 105.2 58.4 66 A GLU C 347 205.3 108.2 56.3 57 A GLU O 347 205.1 109.4 56.3 57 A LYS N 348 205.9 107.6 55.3 56 A LYS CA 348 206.4 108.2 54.1 55 A LYS CB 348 207.3 107.2 53.3 56 A LYS CG 348 208.2 106.4 54.2 56 A LYS CD 348 209.3 107.3 54.8 56 A LYS CE 348 210.4 106.4 55.5 57 A LYS NZ 348 211.0 105.4 54.6 57 A LYS C 348 205.5 108.9 53.2 53 A LYS O 348 205.8 109.9 52.6 53 A ASP N 349 204.2 108.5 53.0 52 A ASP CA 349 203.3 109.1 52.1 51 A ASP CB 349 203.4 108.4 50.7 51 A ASP CG 349 202.9 109.2 49.6 51 A ASP OD1 349 202.8 110.5 49.7 51 A ASP OD2 349 202.6 108.7 48.6 52 A ASP C 349 201.9 109.1 52.6 49 A ASP O 349 201.0 108.7 51.9 49 A THR N 350 201.7 109.6 53.8 48 A THR CA 350 200.4 109.7 54.4 48 A THR CB 350 200.5 110.4 55.8 49 A THR OG1 350 200.9 111.8 55.6 50 A THR CG2 350 201.6 109.7 56.6 49 A THR C 350 199.2 110.3 53.7 47 A THR O 350 198.1 109.9 53.9 46 A ILE N 351 199.5 111.3 52.9 46 A ILE CA 351 198.4 112.0 52.2 44 A ILE CB 351 199.0 113.2 51.3 43 A ILE CG2 351 199.7 112.6 50.1 43 A ILE CG1 351 197.8 114.1 50.9 43 A ILE CD1 351 197.4 115.0 52.1 42 A ILE C 351 197.5 111.0 51.4 43 A ILE O 351 196.3 111.2 51.3 42 A ARG N 352 198.1 109.9 51.0 43 A ARG CA 352 197.3 108.9 50.3 44 A ARG CB 352 197.7 108.7 48.9 43 A ARG CG 352 199.1 108.8 48.5 42 A ARG CD 352 199.3 109.4 47.2 41 A ARG NE 352 200.6 110.2 47.1 42 A ARG CZ 352 200.7 111.5 47.0 43 A ARG NH1 352 199.6 112.3 47.0 42 A ARG NH2 352 201.9 112.1 47.1 43 A ARG C 352 197.4 107.6 51.1 45 A ARG O 352 197.5 106.5 50.5 45 A LYS N 353 197.2 107.7 52.4 46 A LYS CA 353 197.2 106.5 53.3 46 A LYS CB 353 197.0 106.9 54.8 45 A LYS CG 353 195.6 107.5 55.0 45 A LYS CD 353 195.5 108.4 56.3 45 A LYS CE 353 194.1 109.0 56.5 45 A LYS NZ 353 194.0 110.0 57.5 45 A LYS C 353 196.0 105.6 52.8 46 A LYS O 353 196.1 104.4 52.8 46 A GLU N 354 194.9 106.2 52.4 47 A GLU CA 354 193.8 105.5 51.9 48 A GLU CB 354 192.6 106.5 51.6 50 A GLU CG 354 192.0 107.2 52.8 53 A GLU CD 354 191.2 106.2 53.7 55 A GLU OE1 354 191.4 106.2 54.9 56 A GLU OE2 354 190.3 105.5 53.1 56 A GLU C 354 194.1 104.7 50.6 48 A GLU O 354 193.4 103.7 50.4 48 A TYR N 355 195.0 105.1 49.9 47 A TYR CA 355 195.4 104.4 48.6 46 A TYR CB 355 196.0 105.4 47.6 44 A TYR CG 355 196.7 104.7 46.4 41 A TYR CD1 355 195.9 104.2 45.4 40 A TYR CE1 355 196.4 103.4 44.4 39 A TYR CD2 355 198.0 104.6 46.4 40 A TYR CE2 355 198.6 103.8 45.3 40 A TYR CZ 355 197.8 103.3 44.4 39 A TYR OH 355 198.4 102.5 43.4 39 A TYR C 355 196.3 103.3 49.0 47 A TYR O 355 196.1 102.1 48.6 47 A TRP N 356 197.4 103.6 49.6 49 A TRP CA 356 198.4 102.7 50.0 51 A TRP CB 356 199.6 103.4 50.7 52 A TRP CG 356 200.3 104.2 49.7 52 A TRP CD2 356 201.1 103.6 48.6 53 A TRP CE2 356 201.6 104.7 47.9 52 A TRP CE3 356 201.3 102.3 48.1 53 A TRP CD1 356 200.5 105.5 49.6 52 A TRP NE1 356 201.3 105.9 48.6 52 A TRP CZ2 356 202.4 104.6 46.7 52 A TRP CZ3 356 202.0 102.2 47.0 53 A TRP CH2 356 202.6 103.3 46.3 53 A TRP C 356 197.9 101.5 50.9 52 A TRP O 356 198.4 100.4 50.8 52 A ARG N 357 196.9 101.8 51.6 52 A ARG CA 357 196.3 100.7 52.5 53 A ARG CB 357 195.5 101.3 53.6 55 A ARG CG 357 196.3 101.3 54.9 57 A ARG CD 357 196.3 102.6 55.6 58 A ARG NE 357 194.9 103.0 55.9 59 A ARG CZ 357 194.6 104.0 56.7 60 A ARG NH1 357 193.3 104.2 57.0 61 A ARG NH2 357 195.6 104.7 57.3 59 A ARG C 357 195.4 99.8 51.6 52 A ARG O 357 195.4 98.6 51.8 52 A TYR N 358 194.8 100.4 50.6 51 A TYR CA 358 193.9 99.7 49.6 49 A TYR CB 358 193.2 100.6 48.7 49 A TYR CG 358 192.8 99.9 47.4 48 A TYR CD1 358 191.6 99.2 47.4 48 A TYR CE1 358 191.2 98.5 46.3 47 A TYR CD2 358 193.4 100.1 46.2 47 A TYR CE2 358 193.0 99.4 45.0 46 A TYR CZ 358 191.9 98.7 45.1 47 A TYR OH 358 191.5 98.0 44.0 46 A TYR C 358 194.9 98.7 48.9 49 A TYR O 358 194.5 97.6 48.5 49 A ILE N 359 196.1 99.2 48.6 49 A ILE CA 359 197.1 98.4 47.9 49 A ILE CB 359 198.4 99.2 47.6 48 A ILE CG2 359 199.5 98.3 47.1 47 A ILE CG1 359 198.1 100.2 46.5 48 A ILE CD1 359 197.5 99.6 45.3 47 A ILE C 359 197.4 97.2 48.8 51 A ILE O 359 197.6 96.1 48.3 50 A GLY N 360 197.5 97.4 50.1 52 A GLY CA 360 197.8 96.4 51.0 54 A GLY C 360 196.7 95.4 51.0 55 A GLY O 360 196.9 94.2 50.8 56 A ARG N 361 195.4 95.9 51.2 56 A ARG CA 361 194.2 95.1 51.2 57 A ARG CB 361 193.0 96.0 51.4 58 A ARG CG 361 192.4 95.8 52.8 59 A ARG CD 361 192.0 97.1 53.4 59 A ARG NE 361 191.1 97.9 52.6 60 A ARG CZ 361 191.3 99.2 52.3 61 A ARG NH1 361 190.4 99.8 51.5 62 A ARG NH2 361 192.3 99.9 52.8 62 A ARG C 361 194.1 94.2 49.9 58 A ARG O 361 193.7 93.1 50.0 59 A SER N 362 194.3 94.8 48.7 59 A SER CA 362 194.2 94.1 47.5 58 A SER CB 362 194.2 95.0 46.3 58 A SER OG 362 192.9 95.6 46.1 59 A SER C 362 195.3 93.1 47.4 58 A ER O 362 195.1 91.9 47.2 57 A LEU N 363 196.5 93.5 47.6 58 A LEU CA 363 197.7 92.6 47.6 59 A LEU CB 363 198.9 93.4 48.1 58 A LEU CG 363 200.0 93.6 47.1 58 A LEU CD1 363 199.5 94.4 45.9 59 A LEU CD2 363 201.2 94.3 47.7 58 A LEU C 363 197.4 91.5 48.6 59 A LEU O 363 197.9 90.3 48.4 59 A GLN N 364 196.7 91.7 49.6 61 A GLN CA 364 196.3 90.8 50.6 62 A GLN CB 364 195.5 91.4 51.7 63 A GLN CG 364 195.5 90.7 53.0 64 A GLN CD 364 196.8 90.9 53.7 65 A GLN OE1 364 196.9 91.7 54.7 66 A GLN NE2 364 197.9 90.3 53.2 65 A GLN C 364 195.5 89.6 50.0 63 A GLN O 364 195.8 88.5 50.2 64 A SER N 365 194.5 89.9 49.2 65 A SER CA 365 193.8 88.8 48.5 67 A SER CB 365 192.3 89.2 48.4 66 A SER OG 365 192.0 90.3 47.6 67 A SER C 365 194.3 88.4 47.2 69 A SER O 365 193.5 88.0 46.3 69 A LYS N 366 195.6 88.4 47.0 71 A LYS CA 366 196.2 87.9 45.7 73 A LYS CB 366 195.7 88.7 44.5 74 A LYS CG 366 196.1 90.1 44.3 75 A LYS CD 366 194.9 91.0 44.7 77 A LYS CE 366 193.6 90.7 43.9 78 A LYS NZ 366 192.5 91.6 44.4 79 A LYS C 366 197.8 87.8 45.7 73 A LYS OT1 366 198.3 87.2 46.7 73 A LYS OT2 366 198.5 88.4 44.8 73 A LEU CB 523 194.0 121.4 61.8 44 B LEU CG 523 192.7 122.2 62.1 45 B LEU CD1 523 193.0 123.6 61.8 45 B LEU CD2 523 191.6 121.6 61.3 45 B LEU C 523 195.1 119.1 61.5 45 B LEU O 523 196.2 119.4 62.0 44 B LEU N 523 193.6 119.5 63.4 45 B LEU CA 523 193.8 119.8 62.0 44 B TYR N 524 194.9 118.3 60.5 44 B TYR CA 524 196.0 117.5 59.9 44 B TYR CB 524 195.4 116.6 58.8 43 B TYR CG 524 196.4 115.9 58.0 43 B TYR CD1 524 197.1 114.8 58.5 42 B TYR CE1 524 198.1 114.1 57.7 43 B TYR CD2 524 196.7 116.3 56.7 43 B TYR CE2 524 197.7 115.7 55.9 43 B TYR CZ 524 198.3 114.6 56.4 43 B TYR OH 524 199.2 113.9 55.6 41 B TYR C 524 197.1 118.4 59.4 45 B TYR O 524 198.3 118.1 59.6 44 B SER N 525 196.8 119.4 58.6 46 B SER CA 525 197.8 120.2 58.0 48 B SER CB 525 197.2 121.1 56.9 48 B SER OG 525 195.9 121.5 57.3 48 B SER C 525 198.6 121.0 59.1 50 B SER O 525 199.8 121.2 58.9 50 B LEU N 526 197.9 121.3 60.2 52 B LEU CA 526 198.6 122.1 61.2 53 B LEU CB 526 197.6 122.8 62.1 52 B LEU CG 526 197.5 124.3 61.9 52 B LEU CD1 526 198.6 124.8 61.0 53 B LEU CD2 526 196.2 124.7 61.3 52 B LEU C 526 199.4 121.1 62.1 54 B LEU O 526 200.0 121.6 63.1 54 B ARG N 527 199.4 119.8 61.8 55 B ARG CA 527 200.2 118.9 62.6 57 B ARG CB 527 199.8 117.5 62.1 58 B ARG CG 527 200.1 116.4 63.1 58 B ARG CD 527 199.2 115.2 62.9 58 B ARG NE 527 197.7 115.6 63.1 57 B ARG CZ 527 196.7 114.8 62.7 57 B ARG NH1 527 196.9 113.7 62.0 57 B ARG NH2 527 195.5 115.2 62.9 57 B ARG C 527 201.6 119.2 62.4 59 B ARG O 527 202.1 119.6 61.3 59 B PRO N 528 202.4 119.0 63.5 60 B PRO CD 528 202.0 118.7 64.8 61 B PRO CA 528 203.9 119.3 63.5 60 B PRO CB 528 204.3 119.0 64.9 60 B PRO CG 528 203.1 119.3 65.7 61 B PRO C 528 204.7 118.5 62.5 60 B PRO O 528 205.7 119.0 61.9 60 B GLU N 529 204.4 117.2 62.4 61 B GLU CA 529 205.1 116.3 61.5 62 B GLU CB 529 204.7 114.9 61.8 63 B GLU CG 529 203.2 114.6 62.0 65 B GLU CD 529 202.9 114.6 63.5 66 B GLU OE1 529 201.9 113.9 63.9 66 B GLU OE2 529 203.5 115.4 64.3 67 B GLU C 529 204.8 116.7 60.0 62 B GLU O 529 205.6 116.4 59.1 63 B HIS N 530 203.7 117.3 59.8 62 B HIS CA 530 203.3 117.7 58.4 62 B HIS CB 530 201.8 118.3 58.5 62 B HIS CG 530 201.3 118.9 57.2 63 B HIS CD2 530 200.5 118.4 56.2 62 B HIS ND1 530 201.7 120.2 56.8 63 B HIS CE1 530 201.1 120.4 55.7 63 B HIS NE2 530 200.4 119.4 55.3 62 B HIS C 530 204.2 118.7 57.7 60 B HIS O 530 204.1 118.9 56.5 60 B ALA N 531 205.1 119.4 58.5 59 B ALA CA 531 206.0 120.3 57.9 59 B ALA CB 531 206.6 121.2 59.0 59 B ALA C 531 207.1 119.6 57.2 58 B ALA O 531 207.9 120.1 56.4 57 B ARG N1 532 207.2 118.3 57.5 57 B ARG CA 532 208.2 117.4 56.8 57 B ARG CB 532 208.4 116.1 57.5 59 B ARG CG 532 209.4 116.1 58.7 63 B ARG CD 532 208.7 115.8 60.0 66 B ARG NE 532 208.4 114.4 60.2 69 B ARG CZ 532 208.0 113.9 61.4 70 B ARG NH1 532 207.9 114.6 62.5 71 B ARG NH2 532 207.8 112.6 61.5 71 B ARG C 532 207.8 117.2 55.4 56 B ARG O 532 208.7 116.9 54.5 56 B GLU N 533 206.5 117.3 55.1 54 B GLU CA 533 206.0 117.2 53.8 53 B GLU CB 533 204.5 117.0 53.9 52 B GLU CG 533 204.1 115.6 54.5 51 B GLU CD 533 204.6 114.4 53.8 51 B GLU OE1 533 203.8 113.8 53.1 51 B GLU OE2 533 205.8 114.1 53.9 51 B GLU C 533 206.2 118.4 52.9 53 B GLU O 533 205.5 118.6 51.9 53 B ARG N 534 207.3 119.2 53.2 52 B ARG CA 534 207.6 120.3 52.4 50 B ARG CB 534 208.4 121.3 53.3 51 B ARG CG 534 208.2 122.7 53.0 52 B ARG CD 534 206.9 123.2 53.4 53 B ARG NE 534 206.6 124.6 53.0 55 B ARG CZ 534 207.4 125.6 53.4 57 B ARG NH1 534 208.4 125.5 54.1 58 B ARG NH2 534 207.0 126.8 52.9 58 B ARG C 534 208.4 119.8 51.3 49 B ARG O 534 209.1 118.8 51.4 48 B LEU N 535 208.4 120.6 50.2 49 B LEU CA 535 209.1 120.2 49.0 49 B LEU CB 535 208.9 121.3 47.9 47 B LEU CG 535 209.7 121.1 46.6 46 B LEU CD1 535 209.2 119.9 45.8 46 B LEU CD2 535 209.7 122.4 45.7 45 B LEU C 535 210.6 120.0 49.2 49 B LEU O 535 211.2 120.7 50.0 50 B GLN N 536 211.2 119.1 48.4 49 B GLN CA 536 212.6 118.8 48.5 50 B GLN CB 536 212.8 117.4 49.0 51 B GLN CG 536 211.9 117.0 50.1 52 B GLN CD 536 212.5 115.9 51.0 52 B GLN OE1 536 211.7 115.2 51.6 54 B GLN NE2 536 213.8 115.8 50.9 52 B GLN C 536 213.1 119.0 47.1 51 B GLN O 536 213.0 118.1 46.3 52 B ASP N 537 213.8 120.1 46.9 52 B ASP CA 537 214.3 120.4 45.6 52 B ASP CB 537 214.4 122.0 45.4 53 B ASP CG 537 215.7 122.5 45.8 53 B ASP OD1 537 216.4 122.0 46.7 54 B ASP OD2 537 216.1 123.6 45.3 54 B ASP C 537 215.6 119.8 45.1 52 B ASP O 537 216.1 120.1 44.1 52 B ASP N 538 216.1 118.8 45.9 52 B ASP CA 538 217.4 118.1 45.6 52 B ASP CB 538 217.2 117.2 44.4 53 B ASP CG 538 216.1 116.2 44.6 54 B ASP OD1 538 216.2 115.4 45.6 56 B ASP OD2 538 215.2 116.1 43.8 55 B ASP C 538 218.5 119.1 45.4 52 B ASP O 538 219.6 118.7 44.9 51 B SER N 539 218.3 120.3 45.7 53 B SER CA 539 219.3 121.4 45.5 54 B SER CB 539 220.6 121.1 46.2 56 B SER OG 539 220.3 120.9 47.6 58 B SER C 539 219.6 121.6 44.0 53 B SER O 539 220.6 122.1 43.6 54 B VAL N 540 218.6 121.3 43.2 51 B VAL CA 540 218.6 121.5 41.8 49 B VAL CB 540 218.5 120.1 41.0 48 B VAL CG1 540 218.4 120.4 39.5 47 B VAL CG2 540 219.7 119.2 41.3 47 B VAL C 540 217.3 122.3 41.5 48 B VAL O 540 216.2 121.8 41.4 48 B GLU N 541 217.5 123.6 41.4 47 B GLU CA 541 216.4 124.5 41.1 46 B GLU CB 541 216.6 125.9 41.6 48 B GLU CG 541 217.5 126.0 42.8 51 B GLU CD 541 217.3 127.3 43.4 52 B GLU OE1 541 217.8 128.3 42.8 53 B GLU OE2 541 216.7 127.4 44.5 54 B GLU C 541 216.0 124.6 39.7 44 B GLU O 541 216.8 124.7 38.8 45 B THR N 542 214.7 124.7 39.5 42 B THR CA 542 214.1 124.9 38.1 40 B THR CB 542 213.8 123.6 37.5 39 B THR OG1 542 212.9 122.9 38.2 40 B THR CG2 542 215.1 122.8 37.3 39 B THR C 542 212.9 125.8 38.3 38 B THR O 542 212.4 126.1 39.4 38 B VAL N 543 212.3 126.3 37.2 36 B VAL CA 543 211.2 127.1 37.3 35 B VAL CB 543 210.6 127.4 35.9 35 B VAL CG1 543 209.4 128.4 36.0 34 B VAL CG2 543 211.6 128.0 35.0 35 B VAL C 543 210.1 126.4 38.1 34 B VAL O 543 209.4 127.1 38.9 35 B THR N 544 210.0 125.1 38.0 34 B THR CA 544 209.0 124.3 38.7 33 B THR CB 544 209.0 122.8 38.1 33 B THR OG1 544 208.9 122.9 36.7 33 B THR CG2 544 207.9 122.1 38.8 33 B THR C 544 209.1 124.2 40.2 33 B THR O 544 208.1 124.4 40.9 34 B SER N 545 210.3 124.0 40.7 33 B SER CA 545 210.5 123.9 42.2 33 B SER CB 545 211.8 123.2 42.5 33 B SER OG 545 212.9 123.9 41.9 33 B SER C 545 210.4 125.3 42.7 33 B SER O 545 209.7 125.5 43.7 34 B ILE N 546 211.0 126.3 42.0 33 B ILE CA 546 210.9 127.7 42.4 32 B ILE CB 546 211.6 128.5 41.4 32 B ILE CG2 546 211.3 130.0 41.6 31 B ILE CG1 546 213.1 128.2 41.4 32 B ILE CD1 546 213.9 128.8 40.2 34 B ILE C 546 209.5 128.1 42.6 32 B ILE O 546 209.1 128.7 43.6 33 B GLU N 547 208.6 127.8 41.7 32 B GLU CA 547 207.2 128.2 41.7 31 B GLU CB 547 206.5 128.0 40.4 31 B GLU CG 547 207.0 129.0 39.4 30 B GLU CD 547 207.0 130.5 39.9 31 B GLU OE1 547 205.9 130.9 40.3 30 B GLU OE2 547 208.0 131.1 39.9 32 B GLU C 547 206.4 127.4 42.8 31 B GLU O 547 205.5 127.9 43.4 30 B GLN N 548 206.7 126.1 42.8 32 B GLN CA 548 206.0 125.2 43.8 33 B GLN CB 548 206.5 123.7 43.6 30 B GLN CG 548 205.9 122.7 44.6 29 B GLN CD 548 204.4 122.8 44.7 29 B GLN OE1 548 203.9 122.6 45.8 30 B GLN NE2 548 203.8 123.1 43.6 29 B GLN C 548 206.4 125.7 45.2 35 B GLN O 548 205.5 125.8 46.1 36 B ALA N 549 207.6 126.1 45.4 36 B ALA CA 549 208.1 126.6 46.7 37 B ALA CB 549 209.6 126.9 46.6 35 B ALA C 549 207.4 127.9 47.1 37 B ALA O 549 207.0 128.1 48.2 38 B LYS N 550 207.2 128.8 46.1 39 B LYS CA 550 206.5 130.0 46.4 40 B LYS CB 550 206.4 130.9 45.2 41 B LYS CG 550 207.7 131.3 44.6 43 B LYS CD 550 207.5 132.4 43.5 45 B LYS CE 550 208.7 132.6 42.7 46 B LYS NZ 550 208.5 133.5 41.5 47 B LYS C 550 205.1 129.8 46.9 40 B LYS O 550 204.6 130.4 47.8 40 B VAL N 551 204.5 128.8 46.3 41 B VAL CA 551 203.1 128.4 46.7 41 B VAL CB 551 202.5 127.4 45.8 41 B VAL CG1 551 201.3 126.7 46.3 41 B VAL CG2 551 202.1 128.1 44.5 42 B VAL C 551 203.1 127.9 48.1 42 B VAL O 551 202.4 128.4 49.0 42 B GLU N 552 203.9 126.8 48.4 43 B GLU CA 552 204.0 126.2 49.7 43 B GLU CB 552 205.1 125.2 49.8 42 B GLU CG 552 204.8 123.9 49.0 39 B GLU CD 552 205.8 122.9 49.1 39 B GLU OE1 552 206.9 123.1 49.6 38 B GLU OE2 552 205.5 121.7 48.7 39 B GLU C 552 204.2 127.3 50.8 45 B GLU O 552 203.4 127.3 51.8 46 B GLU N 553 205.1 128.2 50.6 48 B GLU CA 553 205.4 129.3 51.5 49 B GLU CB 553 206.4 130.2 51.0 52 B GLU CG 553 206.8 131.3 51.9 56 B GLU CD 553 208.3 131.2 52.3 59 B GLU OE1 553 208.6 130.3 53.1 60 B GLU OE2 553 209.1 132.1 51.8 60 B GLU C 553 204.2 130.0 51.9 49 B GLU O 553 203.9 130.2 53.1 49 B LYS N 554 203.4 130.5 51.0 49 B LYS CA 554 202.2 131.2 51.3 51 B LYS CB 554 201.5 131.7 50.0 53 B LYS CG 554 202.4 132.4 49.0 57 B LYS CD 554 201.6 132.8 47.8 61 B LYS CE 554 202.4 133.7 46.9 63 B LYS NZ 554 201.5 134.5 46.0 65 B LYS C 554 201.2 130.4 52.1 51 B LYS O 554 200.6 130.8 53.0 51 B ILE N 555 201.2 129.1 51.7 50 B ILE CA 555 200.3 128.1 52.4 49 B ILE CB 555 200.3 126.8 51.7 49 B ILE CG2 555 199.3 125.8 52.4 48 B ILE CG1 555 199.8 126.9 50.2 49 B ILE CD1 555 198.4 127.5 50.1 48 B ILE C 555 200.8 128.0 53.8 50 B ILE O 555 200.0 128.0 54.8 49 B GLN N 556 202.1 127.8 54.0 50 B GLN CA 556 202.7 127.7 55.3 51 B GLN CB 556 204.3 127.7 55.1 51 B GLN CG 556 205.0 127.5 56.4 52 B GLN CD 556 204.7 126.2 57.1 53 B GLN OE1 556 205.6 125.3 57.1 53 B GLN NE2 556 203.6 126.1 57.8 52 B GLN C 556 202.3 128.8 56.1 52 B GLN O 556 201.9 128.7 57.3 54 B GLU N 557 202.4 130.0 55.6 53 B GLU CA 557 202.0 131.2 56.3 54 B GLU CB 557 202.4 132.5 55.5 57 B GLU CG 557 203.9 132.5 55.1 60 B GLU CD 557 204.4 133.8 54.3 62 B GLU OE1 557 203.5 134.6 53.9 63 B GLU OE2 557 205.6 133.9 54.0 62 B GLU C 557 200.6 131.3 56.7 53 B GLU O 557 200.2 132.0 57.6 54 B VAL N 558 199.7 130.5 56.0 53 B VAL CA 558 198.3 130.5 56.2 52 B VAL CB 558 197.5 130.0 55.0 52 B VAL CG1 558 196.0 129.7 55.4 51 B VAL CG2 558 197.5 131.0 53.9 52 B VAL C 558 198.0 129.5 57.4 52 B VAL O 558 197.3 129.8 58.3 52 B PHE N 559 198.6 128.3 57.3 52 B PHE CA 559 198.5 127.3 58.3 51 B PHE CB 559 199.3 126.1 57.9 49 B PHE CG 559 198.7 125.4 56.8 47 B PHE CD1 559 199.4 124.4 56.1 47 B PHE CD2 559 197.4 125.6 56.4 47 B PHE CE1 559 198.8 123.7 55.0 46 B PHE CE2 559 196.8 124.9 55.3 46 B PHE CZ 559 197.5 123.9 54.7 46 B PHE C 559 196.9 127.9 59.7 52 B PHE O 559 198.1 127.8 60.7 52 B SER N 560 200.1 128.4 59.8 54 B SER CA 560 200.6 129.0 61.0 56 B SER CB 560 202.1 129.3 60.8 55 B SER OG 560 202.8 128.1 60.5 55 B SER C 560 199.9 130.3 61.5 59 B SER O 560 200.2 130.8 62.5 59 B SER N 561 199.0 130.8 60.7 62 B SER CA 561 198.3 132.0 61.1 65 B SER CB 561 197.3 132.5 60.1 65 B SER OG 561 196.3 131.6 59.9 65 B SER C 561 197.6 131.7 62.4 68 B SER O 561 197.5 132.6 63.3 68 B TYR N 562 197.1 130.5 62.5 71 B TYR CA 562 196.4 130.1 63.7 74 B TYR CB 562 195.7 128.7 63.5 74 B TYR CG 562 194.6 128.8 62.4 74 B TYR CD1 562 194.9 128.3 61.1 74 B TYR CE1 562 193.9 128.4 60.1 75 B TYR CD2 562 193.4 129.5 62.7 75 B TYR CE2 562 192.5 129.6 61.7 75 B TYR CZ 562 192.7 129.1 60.4 75 B TYR OH 562 191.7 129.3 59.5 76 B TYR C 562 197.3 130.0 64.9 76 B TYR O 562 197.1 130.6 66.0 75 B LYS N 563 198.4 129.2 64.7 78 B LYS CA 563 199.4 129.0 65.7 81 B LYS CB 563 200.3 127.8 65.3 81 B LYS CG 563 199.6 126.6 64.8 82 B LYS CD 563 200.4 125.4 64.4 83 B LYS CE 563 202.0 125.7 64.3 83 B LYS NZ 563 202.8 124.5 64.4 83 B LYS C 563 200.2 130.3 65.9 82 B LYS O 563 201.5 130.2 65.9 82 B PHE N 564 199.5 131.4 66.1 84 B PHE CA 564 200.2 132.7 66.2 87 B PHE CB 564 199.8 133.5 64.9 90 B PHE CG 564 200.2 134.9 65.0 93 B PHE CD1 564 201.5 135.3 65.1 94 B PHE CD2 564 199.2 135.9 64.9 93 B PHE CE1 564 201.9 136.7 65.1 95 B PHE CE2 564 199.5 137.3 64.9 94 B PHE CZ 564 200.9 137.7 65.0 95 B PHE C 564 199.8 133.4 67.5 87 B PHE O 564 199.0 134.4 67.4 88 B ASN N 565 200.3 132.9 68.6 87 B ASN CA 565 200.0 133.5 69.9 86 B ASN CB 565 200.9 134.7 70.2 88 B ASN CG 565 202.3 134.3 70.8 90 B ASN OD1 565 202.6 133.2 70.9 91 B ASN ND2 565 203.0 135.4 71.1 91 B ASN C 565 198.6 134.0 70.0 85 B ASN O 565 198.4 135.0 70.7 84 B HIS N 566 197.7 133.4 69.4 84 B HIS CA 566 196.3 133.9 69.4 83 B HIS CB 566 196.0 134.4 67.9 85 B HIS CG 566 196.0 135.9 67.8 88 B HIS CD2 566 195.0 136.8 68.0 88 B HIS ND1 566 197.2 136.6 67.6 89 B HIS CE1 566 196.9 137.9 67.6 89 B HIS NE2 566 195.6 138.1 67.8 89 B HIS C 566 195.2 133.1 69.8 80 B HIS O 566 194.9 133.0 71.0 79 B LEU N 567 194.5 132.5 68.9 79 B LEU CA 567 193.3 131.7 69.2 78 B LEU CB 567 192.1 132.3 68.5 77 B LEU CG 567 192.2 133.5 67.6 77 B LEU CD1 567 192.6 134.8 68.4 76 B LEU CD2 567 193.2 133.3 66.4 76 B LEU C 567 193.5 130.2 68.7 77 B LEU O 567 194.6 129.8 68.4 77 B VAL N 568 192.4 129.5 68.7 76 B VAL CA 568 192.4 128.1 68.3 75 B VAL CB 568 191.4 127.3 69.2 75 B VAL CG1 568 191.8 125.8 69.1 76 B VAL CG2 568 191.5 127.7 70.6 75 B VAL C 568 191.8 128.1 66.8 74 B VAL O 568 190.9 128.9 66.5 75 B PRO N 569 192.4 127.2 65.9 73 B PRO CD 569 193.5 126.3 66.0 73 B PRO CA 569 191.8 127.3 64.6 72 B PRO CB 569 192.7 126.2 63.8 72 B PRO CG 569 193.2 125.3 64.9 72 B PRO C 569 190.3 126.9 64.6 71 B PRO O 569 189.9 125.9 65.2 71 B ARG N 570 189.5 127.8 64.0 71 B ARG CA 570 188.1 127.7 63.9 70 B ARG CB 570 187.4 128.9 64.4 72 B ARG CG 570 187.3 129.0 65.9 75 B ARG CD 570 186.1 128.3 66.5 78 B ARG NE 570 186.1 126.9 66.3 80 B ARG CZ 570 185.2 126.1 66.9 81 B ARG NH1 570 184.3 126.6 67.8 81 B ARG NH2 570 185.2 124.8 66.6 81 B ARG C 570 187.8 127.5 62.5 68 B ARG O 570 187.5 128.4 61.7 67 B LEU N 571 187.8 126.2 62.0 64 B LEU CA 571 187.5 126.0 60.6 60 B LEU CB 571 187.9 124.6 60.1 60 B LEU CG 571 189.2 124.6 59.3 59 B LEU CD1 571 190.4 125.0 60.1 59 B LEU CD2 571 189.4 123.2 58.6 59 B LEU C 571 186.0 126.2 60.4 59 B LEU O 571 185.1 125.6 61.1 59 B VAL N 572 185.6 127.2 59.6 57 B VAL CA 572 184.2 127.6 59.4 55 B VAL CB 572 183.9 128.9 60.1 56 B VAL CG1 572 182.5 129.4 59.8 55 B VAL CG2 572 184.0 128.7 61.6 56 B VAL C 572 184.1 127.9 57.9 55 B VAL O 572 185.1 128.2 57.2 56 B LEU N 573 182.9 127.7 57.4 52 B LEU CA 573 182.6 128.0 56.0 50 B LEU CB 573 181.9 126.8 55.3 48 B LEU CG 573 181.3 127.1 53.9 47 B LEU CD1 573 182.5 127.1 53.0 47 B LEU CD2 573 180.3 126.1 53.6 47 B LEU C 573 181.7 129.2 56.0 50 B LEU O 573 180.5 129.2 56.4 49 B GLN N 574 182.2 130.4 55.5 49 B GLN CA 574 181.5 131.6 55.5 49 B GLN CB 574 182.4 132.7 54.9 50 B GLN CG 574 183.8 132.7 55.5 51 B GLN CD 574 183.8 132.7 57.1 52 B GLN OE1 574 184.7 132.1 57.7 53 B GLN NE2 574 182.8 133.4 57.7 52 B GLN C 574 180.2 131.6 54.6 49 B GLN O 574 180.0 132.5 53.8 50 B ARG N 575 179.3 130.8 55.0 49 B ARG CA 575 178.0 130.6 54.2 50 B ARG CB 575 177.0 129.8 55.1 50 B ARG CG 575 177.4 128.4 55.3 51 B ARG CD 575 176.3 127.6 56.0 51 B ARG NE 575 176.5 126.2 55.9 51 B ARG CZ 575 175.9 125.4 55.0 51 B ARG NH1 575 175.0 126.0 54.2 51 B ARG NH2 575 176.1 124.1 55.0 51 B ARG C 575 177.3 131.9 53.8 51 B ARG O 575 176.9 132.0 52.7 50 B GLU N 576 177.0 132.7 54.8 51 B GLU CA 576 176.3 134.0 54.6 52 B GLU CB 576 176.0 134.7 55.9 54 B GLU CG 576 175.7 133.8 57.1 56 B GLU CD 576 174.5 132.8 56.7 58 B GLU OE1 576 173.4 133.2 56.3 59 B GLU OE2 576 174.7 131.5 57.0 59 B GLU C 576 177.1 134.9 53.6 50 B GLU O 576 176.5 135.4 52.7 49 B LYS N 577 178.4 135.0 53.8 48 B LYS CA 577 179.2 135.8 53.0 47 B LYS CB 577 180.6 135.8 53.5 48 B LYS CG 577 181.1 137.2 53.8 49 B LYS CD 577 180.3 137.9 54.9 51 B LYS CE 577 180.1 139.4 54.6 53 B LYS NZ 577 179.0 139.7 53.5 53 B LYS C 577 179.1 135.2 51.5 45 B LYS O 577 178.7 136.0 50.6 45 B HIS N 578 179.3 133.9 51.3 42 B HIS CA 578 179.3 133.3 50.0 39 B HIS CB 578 179.5 131.8 50.1 35 B HIS CG 578 180.8 131.4 50.7 31 B HIS CD2 578 181.3 130.2 51.2 31 B HIS ND1 578 181.9 132.3 50.8 31 B HIS CE1 578 182.9 131.7 51.4 30 B HIS NE2 578 182.6 130.4 51.6 30 B HIS C 578 177.8 133.5 49.5 40 B HIS O 578 177.7 133.6 48.3 40 B PHE N 579 176.8 133.4 50.3 40 B PHE CA 579 175.5 133.5 49.9 41 B PHE CB 579 174.5 133.3 51.1 40 B PHE CG 579 173.1 133.5 50.7 41 B PHE CD1 579 172.4 132.6 50.0 41 B PHE CD2 579 172.5 134.8 51.0 42 B PHE CE1 579 171.1 132.8 49.6 41 B PHE CE2 579 171.2 135.0 50.6 42 B PHE CZ 579 170.5 134.1 49.9 42 B PHE C 579 175.1 134.9 49.3 43 B PHE O 579 174.4 134.9 48.2 43 B HIS N 580 175.5 135.9 49.9 46 B HIS CA 580 175.2 137.3 49.4 48 B HIS CB 580 175.7 138.3 50.4 52 B HIS CG 580 175.2 138.0 51.8 56 B HIS CD2 580 174.0 137.7 52.3 57 B HIS ND1 580 176.1 138.0 52.9 58 B HIS CE1 580 175.5 137.7 54.0 58 B HIS NE2 580 174.2 137.5 53.7 58 B HIS C 580 176.0 137.5 48.1 47 B HIS O 580 175.6 138.3 47.3 47 B TYR N 581 177.2 136.9 48.0 46 B TYR CA 581 178.0 137.0 46.8 45 B TYR CB 581 179.4 136.3 47.1 45 B TYR CG 581 180.3 136.3 45.9 46 B TYR CD1 581 180.5 137.3 45.1 47 B TYR CE1 581 181.4 137.3 44.0 47 B TYR CD2 581 181.0 135.1 45.7 47 B TYR CE2 581 181.8 135.0 44.6 46 B TYR CZ 581 182.0 136.0 43.7 47 B TYR OH 581 182.9 135.9 42.7 47 B TYR C 581 177.3 136.4 45.6 45 B TYR O 581 177.1 137.0 44.6 44 B LEU N 582 176.8 135.1 45.9 44 B LEU CA 582 176.2 134.3 44.9 43 B LEU CB 582 175.9 132.9 45.4 41 B LEU CG 582 177.2 132.1 45.6 40 B LEU CD1 582 177.0 131.1 46.7 40 B LEU CD2 582 177.6 131.5 44.3 40 B LEU C 582 174.8 135.0 44.5 45 B LEU O 582 174.5 135.0 43.3 45 B LYS N 583 174.2 135.5 45.5 48 B LYS CA 583 172.9 136.2 45.4 51 B LYS CB 583 172.4 136.5 46.8 53 B LYS CG 583 171.2 137.4 46.9 56 B LYS CD 583 171.1 138.1 48.3 58 B LYS CE 583 170.0 139.2 48.3 59 B LYS NZ 583 168.6 138.7 48.3 60 B LYS C 583 172.9 137.4 44.5 51 B LYS O 583 171.8 137.7 43.8 51 B ARG N 584 173.9 138.2 44.4 52 B ARG CA 584 173.9 139.5 43.6 53 B ARG CB 584 174.7 140.6 44.2 SS B ARG CG 584 174.0 142.0 43.9 59 B ARG CD 584 174.9 143.2 43.9 62 B ARG NE 584 175.5 143.4 42.6 66 B ARG CZ 584 176.6 144.2 42.4 67 B ARG NH1 584 177.2 144.8 43.5 68 B ARG NH2 584 177.2 144.3 41.2 67 B ARG C 584 174.5 139.1 42.2 51 B ARG O 584 174.1 139.7 41.2 50 B GLY N 585 175.5 138.3 42.2 50 B GLY CA 585 176.1 137.9 40.9 49 B GLY C 585 175.1 137.1 40.1 47 B GLY O 585 175.3 137.0 38.8 47 B LEU N 586 174.1 136.5 40.7 46 B LEU CA 586 173.1 135.8 39.9 45 B LEU CB 586 172.3 134.9 40.8 45 B LEU CG 586 171.2 134.0 40.2 45 B LEU CD1 586 171.8 133.0 39.2 44 B LEU CD2 586 170.5 133.2 41.3 44 B LEU C 586 172.2 136.9 39.2 44 B LEU O 586 171.5 136.5 38.2 45 B ARG N 587 172.3 138.1 39.6 44 B ARG CA 587 171.5 139.2 39.0 43 B ARG CB 587 170.7 140.0 40.0 44 B ARG CG 587 169.2 139.8 40.0 46 B ARG CD 587 168.8 138.3 40.3 48 B ARG NE 587 167.4 138.1 40.6 51 B ARG CZ 587 166.4 138.2 39.8 51 B ARG NH1 587 166.6 138.4 38.5 51 B ARG NH2 587 165.2 137.9 40.2 52 B ARG C 587 172.3 140.1 38.1 42 B ARG O 587 171.8 140.4 37.0 41 B GLN N 588 173.5 140.4 38.5 41 B GLN CA 588 174.3 141.3 37.8 41 B GLN CB 588 173.9 142.7 37.8 43 B GLN CG 588 174.0 143.3 39.2 47 B GLN CD 588 173.7 144.7 39.3 49 B GLN OE1 588 173.1 145.3 38.3 49 B GLN NE2 588 174.1 145.4 40.3 50 B GLN C 588 175.8 141.2 38.2 39 B GLN O 588 176.1 140.9 39.3 39 B LEU N 589 176.7 141.4 37.2 37 B LEU CA 589 178.1 141.3 37.4 35 B LEU CB 589 178.7 140.1 36.7 34 B LEU CG 589 178.0 138.7 37.0 32 B LEU CD1 589 177.9 137.9 35.7 32 B LEU CD2 589 178.7 138.0 38.1 31 B LEU C 589 178.8 142.5 36.8 34 B LEU O 589 178.2 143.1 35.8 33 B THR N 590 179.9 142.9 37.3 34 B THR CA 590 180.6 144.1 36.8 34 B THR CB 590 181.7 144.5 37.8 35 B THR OG1 590 182.8 143.6 37.8 36 B THR CG2 590 181.2 144.7 39.1 36 B THR C 590 181.3 143.7 35.5 35 B THR O 590 181.3 142.5 35.1 35 B ASP N 591 181.8 144.6 34.7 34 B ASP CA 591 182.4 144.4 33.4 34 B ASP CB 591 182.6 145.6 32.7 34 B ASP CG 591 183.5 146.6 33.4 36 B ASP OD1 591 183.7 147.7 32.8 36 B ASP OD2 591 184.0 146.3 34.5 36 B ASP C 591 183.7 143.5 33.5 35 B ASP O 591 184.2 143.2 32.5 37 B ALA N 592 184.1 143.2 34.7 34 B ALA CA 592 185.3 142.3 34.8 33 B ALA CB 592 185.7 142.2 36.2 33 B ALA C 592 184.9 141.0 34.2 33 B ALA O 592 185.8 140.2 33.8 33 B TYR N 593 183.6 140.7 34.1 32 B TYR CA 593 183.1 139.5 33.5 31 B TYR CB 593 181.8 139.1 34.3 31 B TYR CG 593 182.1 138.4 35.5 31 B TYR CD1 593 182.2 139.0 36.8 32 B TYR CE1 593 182.6 138.3 37.9 32 B TYR CD2 593 182.4 137.0 35.5 31 B TYR CE2 593 182.9 136.3 36.6 31 B TYR CZ 593 183.0 137.0 37.8 32 B TYR OH 593 183.4 136.4 38.9 32 B TYR C 593 182.8 139.6 32.0 32 B TYR O 593 182.2 138.7 31.5 32 B GLU N 594 183.2 140.7 31.4 31 B GLU CA 594 183.0 140.8 29.9 29 B GLU CB 594 183.6 142.1 29.4 30 B GLU CG 594 182.8 143.3 29.8 31 B GLU CD 594 183.5 144.6 29.3 33 B GLU OE1 594 182.7 145.5 29.1 33 B GLU OE2 594 184.7 144.6 29.2 34 B GLU C 594 183.7 139.6 29.3 27 B GLU O 594 183.1 139.0 28.4 27 B CYS N 595 184.8 139.1 29.8 25 B CYS CA 595 185.5 138.0 29.3 23 B CYS CB 595 186.9 137.8 30.0 22 B CYS SG 595 186.8 137.3 31.8 22 B CYS C 595 184.7 136.7 29.4 23 B CYS O 595 185.1 135.7 28.7 22 B LEU N 596 183.6 136.7 30.1 22 B LEU CA 596 182.8 135.5 30.3 21 B LEU CB 596 182.6 135.1 31.8 21 B LEU CG 596 183.8 134.2 32.3 21 B LEU CD1 596 183.8 134.2 33.8 20 B LEU CD2 596 183.7 132.8 31.9 20 B LEU C 596 181.4 135.9 29.7 22 B LEU O 596 180.4 135.2 29.9 22 B ASP N 597 181.4 136.8 28.7 24 B ASP CA 597 180.1 137.2 28.1 25 B ASP CB 597 180.4 138.4 27.2 24 B ASP CG 597 179.1 138.9 26.5 24 B ASP OD1 597 178.0 138.9 27.1 24 B ASP OD2 597 179.2 139.3 25.3 25 B ASP C 597 179.6 136.1 27.1 27 B ASP O 597 178.5 136.2 26.6 29 B ALA N 598 180.4 135.0 26.9 28 B ALA CA 598 180.0 133.9 26.1 28 B ALA CB 598 181.0 133.7 24.9 28 B ALA C 598 179.9 132.6 26.9 29 B ALA O 598 179.8 131.5 26.3 29 B SER N 599 179.8 132.7 28.2 30 B SER CA 599 179.7 131.6 29.1 29 B SER CB 599 181.0 131.3 29.8 28 B SER OG 599 182.1 131.3 28.8 28 B SER C 599 178.6 131.9 30.1 29 B SER O 599 178.7 131.6 31.3 30 B ARG N 600 177.6 132.6 29.7 29 B ARG CA 600 176.5 133.0 30.7 30 B ARG CB 600 175.7 134.2 30.2 30 B ARG CG 600 176.5 135.4 30.0 30 B ARG CD 600 175.7 136.6 29.4 31 B ARG NE 600 174.8 137.1 30.4 32 B ARG CZ 600 173.8 137.8 30.1 32 B ARG NH1 600 173.5 138.2 28.8 33 B ARG NH2 600 172.9 138.2 31.0 34 B ARG C 600 175.8 131.9 31.3 31 B ARG O 600 175.4 131.9 32.4 33 B PRO N 601 175.6 130.8 30.5 30 B PRO CD 601 175.5 130.6 29.1 30 B PRO CA 601 174.8 129.7 31.2 28 B PRO CB 601 174.5 128.7 30.1 28 B PRO CG 601 174.3 129.6 28.9 29 B PRO C 601 175.8 129.1 32.2 28 B PRO O 601 175.4 128.6 33.2 30 B TRP N 602 177.1 129.2 32.0 27 B TRP CA 602 178.0 128.7 33.0 26 B TRP CB 602 179.5 128.8 32.6 25 B TRP CG 602 179.9 127.8 31.7 26 B TRP CD2 602 180.2 126.4 32.0 26 B TRP CE2 602 180.6 125.8 30.9 26 B TRP CE3 602 180.1 125.7 33.2 26 B TRP CD1 602 180.2 127.9 30.4 25 B TRP NE1 602 180.6 126.7 29.9 26 B TRP CZ2 602 181.0 124.4 30.8 26 B TRP CZ3 602 180.5 124.3 33.2 26 B TRP CH2 602 180.9 123.7 32.0 26 B TRP C 602 177.8 129.5 34.3 27 B TRP O 602 177.8 128.9 35.4 28 B LEU N 603 177.6 130.8 34.1 28 B LEU CA 603 177.4 131.6 35.3 28 B LEU CB 603 177.4 133.1 35.0 29 B LEU CG 603 178.9 133.5 34.7 30 B LEU CD1 603 178.9 134.9 34.0 30 B LEU CD2 603 179.7 133.5 36.0 29 B LEU C 603 176.1 131.2 36.1 29 B LEU O 603 176.1 131.3 37.3 30 B CYS N 604 175.1 130.8 35.3 28 B CYS CA 604 173.8 130.4 36.0 28 B CYS CB 604 172.7 130.2 35.0 28 B CYS SG 604 172.2 131.6 34.0 31 B CYS C 604 174.2 129.1 36.7 28 B CYS O 604 174.0 129.1 37.9 29 B TYR N 605 174.7 128.1 36.0 26 B TYR CA 605 175.1 126.9 36.7 24 B TYR CB 605 175.7 125.9 35.7 23 B TYR CG 605 176.3 124.7 36.4 23 B TYR CD1 605 175.5 123.7 37.0 23 B TYR CE1 605 176.1 122.7 37.7 22 B TYR CD2 605 177.7 124.5 36.3 22 B TYR CE2 605 178.3 123.5 37.0 22 B TYR CZ 605 177.5 122.5 37.6 22 B TYR OH 605 178.2 121.5 38.2 24 B TYR C 605 176.0 127.0 37.9 25 B TYR O 605 175.7 126.5 39.0 25 B TRP N 606 177.1 127.7 37.7 27 B TRP CA 606 178.1 127.9 38.8 27 B TRP CB 606 179.2 128.8 38.3 27 B TRP CG 606 180.2 128.3 37.2 27 B TRP CD2 606 180.9 129.1 36.3 28 B TRP CE2 606 181.7 128.2 35.5 28 B TRP CE3 606 181.0 130.5 36.0 29 B TRP CD1 606 180.5 127.0 37.0 27 B TRP NE1 606 181.4 127.0 35.9 27 B TRP CZ2 606 182.5 128.7 34.4 28 B TRP CZ3 606 181.8 131.0 35.0 29 B TRP CH2 606 182.6 130.1 34.2 28 B TRP C 606 177.4 128.4 40.0 28 B TRP O 606 177.5 127.9 41.1 28 B ILE N 607 176.6 129.5 39.8 30 B ILE CA 607 175.9 130.1 40.9 30 B ILE CB 607 175.4 131.6 40.6 29 B ILE CG2 607 174.5 132.1 41.7 29 B ILE CG1 607 176.6 132.4 40.3 28 B ILE CD1 607 176.3 133.6 39.4 28 B ILE C 607 174.7 129.3 41.5 31 B ILE O 607 174.7 129.0 42.7 33 B LEU N 608 173.8 128.9 40.7 31 B LEU CA 608 172.6 128.0 41.1 29 B LEU CB 608 171.7 127.7 39.9 28 B LEU CG 608 170.4 128.4 39.9 28 B LEU CD1 608 170.4 129.8 40.5 28 B LEU CD2 608 169.9 128.5 38.4 29 B LEU C 608 173.1 126.8 41.7 30 B LEU O 608 172.4 126.2 42.5 33 B HIS N 609 174.3 126.3 41.3 30 B HIS CA 609 174.8 125.0 41.9 29 B HIS CB 609 175.7 124.3 41.0 27 B HIS CG 609 176.3 123.1 41.6 26 B HIS CD2 609 177.6 122.7 41.8 26 B HIS ND1 609 175.6 122.1 42.2 25 B HIS CE1 609 176.4 121.1 42.7 26 B HIS NE2 609 177.6 121.5 42.5 26 B HIS C 609 175.4 125.3 43.3 30 B HIS O 609 175.4 124.5 44.2 32 B SER N 610 176.1 126.4 43.4 32 B SER CA 610 176.8 126.8 44.7 34 B SER CB 610 177.6 128.0 44.5 34 B SER OG 610 178.6 127.8 43.5 35 B SER C 610 175.7 127.0 45.8 34 B SER O 610 175.8 126.6 46.9 35 B LEU N 611 174.6 127.7 45.4 35 B LEU CA 611 173.5 127.9 46.3 36 B LEU CB 611 172.4 128.7 45.6 34 B LEU CG 611 172.8 130.1 45.2 33 B LEU CD1 611 171.6 130.8 44.4 34 B LEU CD2 611 173.1 130.9 46.4 33 B LEU C 611 173.0 126.6 46.7 38 B LEU O 611 172.8 126.3 47.9 40 B GLU N 612 172.8 125.7 45.7 39 B GLU CA 612 172.3 124.3 46.0 40 B GLU CB 612 172.3 123.5 44.7 42 B GLU CG 612 171.9 122.1 44.8 44 B GLU CD 612 172.6 121.2 43.8 45 B GLU OE1 612 173.3 120.3 44.3 44 B GLU OE2 612 172.4 121.4 42.6 45 B GLU C 612 173.1 123.6 47.0 41 B GLU O 612 172.6 123.0 48.0 42 B LEU N 613 174.5 123.7 46.9 41 B LEU CA 613 175.3 123.1 47.8 41 B LEU CB 613 176.8 123.2 47.4 40 B LEU CG 613 177.1 122.3 46.1 40 B LEU CD1 613 178.4 122.9 45.5 40 B LEU CD2 613 177.4 120.9 46.6 39 B LEU C 613 175.2 123.7 49.2 43 B LEU O 613 175.1 123.0 50.2 43 B LEU N 614 175.1 125.1 49.2 45 B LEU CA 614 174.9 125.8 50.4 47 B LEU CB 614 175.2 127.3 50.2 45 B LEU CG 614 176.6 127.7 49.7 45 B LEU CD1 614 176.6 129.1 49.3 45 B LEU CD2 614 177.7 127.5 50.7 44 B LEU C 614 173.5 125.8 51.0 49 B LEU O 614 173.1 126.5 51.8 48 B ASP N 615 172.7 124.9 50.4 52 B ASP CA 615 171.3 124.7 50.8 54 B ASP CB 615 171.2 124.1 52.2 55 B ASP CG 615 169.9 123.3 52.4 55 B ASP OD1 615 169.0 123.4 51.6 55 B ASP OD2 615 169.8 122.8 53.5 56 B ASP C 615 170.5 126.0 50.7 56 B ASP O 615 169.4 126.1 51.3 58 B GLU N 616 171.0 127.0 50.0 57 B GLU CA 616 170.2 128.2 49.9 59 B GLU CB 616 171.2 129.4 49.6 61 B GLU CG 616 172.4 129.4 50.6 64 B GLU CD 616 172.1 130.0 51.9 65 B GLU OE1 616 171.0 130.4 52.2 67 B GLU OE2 616 173.1 130.1 52.7 66 B GLU C 616 169.2 128.0 48.7 60 B GLU O 616 169.5 127.3 47.8 60 B PRO N 617 168.0 128.5 48.8 61 B PRO CD 617 167.7 129.5 49.9 62 B PRO CA 617 166.9 128.4 47.9 62 B PRO CB 617 165.7 128.9 48.7 62 B PRO CG 617 166.3 130.1 49.4 63 B PRO C 617 167.0 129.2 46.6 62 B PRO O 617 167.6 130.3 46.5 62 B ILE N 618 166.2 128.7 45.6 62 B ILE CA 618 166.1 129.3 44.3 62 B ILE CB 618 166.5 128.3 43.1 62 B ILE CG2 618 166.1 128.9 41.7 62 B ILE CG1 618 168.0 127.9 43.2 62 B ILE CD1 618 168.4 127.0 44.3 62 B ILE C 618 164.6 129.8 44.0 61 B ILE O 618 163.8 129.1 43.5 61 B PRO N 619 164.3 131.0 44.5 60 B PRO CD 619 165.2 131.9 45.2 60 B PRO CA 619 162.9 131.6 44.4 59 B PRO CB 619 163.2 133.0 44.7 59 B PRO CG 619 164.2 133.0 45.7 59 B PRO C 619 162.3 131.3 43.1 59 B PRO O 619 162.9 131.6 42.1 59 B GLN N 620 161.0 131.0 43.2 59 B GLN CA 620 160.2 130.7 42.0 60 B GLN CB 620 158.8 130.4 42.5 62 B GLN CG 620 158.7 129.5 43.8 64 B GLN CD 620 157.4 128.7 43.9 65 B GLN OE1 620 156.4 128.9 43.2 66 B GLN NE2 620 157.4 127.9 44.9 65 B GLN C 620 160.3 131.7 40.9 59 B GLN O 620 160.3 131.4 39.7 59 B ILE N 621 160.6 133.0 41.4 57 B ILE CA 621 160.7 134.1 40.4 56 B ILE CB 621 160.4 135.5 41.2 57 B ILE CG2 621 160.4 136.6 40.1 57 B ILE CG1 621 159.1 135.4 42.0 58 B ILE CD1 621 159.2 134.7 43.4 58 B ILE C 621 162.1 134.2 39.7 54 B ILE O 621 162.2 134.5 38.6 52 B VAL N 622 163.1 134.0 40.5 53 B VAL CA 622 164.4 134.1 39.9 52 B VAL CB 622 165.6 134.1 41.0 52 B VAL CG1 622 165.8 132.7 41.6 52 B VAL CG2 622 166.8 134.6 40.3 53 B VAL C 622 164.6 132.9 39.0 52 B VAL O 622 165.2 133.0 37.9 52 B ALA N 623 164.0 131.7 39.4 51 B ALA CA 623 164.0 130.5 38.6 50 B ALA CB 623 163.3 129.4 39.3 49 B ALA C 623 163.4 130.8 37.2 50 B ALA O 623 164.0 130.4 36.2 51 B THR N 624 162.2 131.3 37.2 49 B THR CA 624 161.6 131.6 35.9 47 B THR CB 624 160.2 132.4 36.1 46 B THR OG1 624 159.4 131.5 36.9 47 B THR CG2 624 159.6 132.6 34.8 46 B THR C 624 162.5 132.5 35.0 47 B THR O 624 162.6 132.2 33.8 48 B ASP N 625 163.1 133.5 35.7 47 B ASP CA 625 164.0 134.4 34.9 46 B ASP CB 625 164.5 135.5 35.9 49 B ASP CG 625 163.5 136.4 36.5 50 B ASP OD1 625 162.5 136.8 35.8 49 B ASP OD2 625 163.6 136.9 37.7 50 B ASP C 625 165.1 133.6 34.3 44 B ASP O 625 165.4 133.7 33.1 43 B VAL N 626 165.7 132.8 35.2 41 B VAL CA 626 166.8 131.9 34.7 40 B VAL CB 626 167.2 130.9 35.7 40 B VAL CG1 626 168.2 130.0 35.1 40 B VAL CG2 626 167.9 131.6 36.9 40 B VAL C 626 166.2 131.1 33.5 41 B VAL O 626 166.9 131.1 32.4 43 B CYS N 627 165.0 130.6 33.6 40 B CYS CA 627 164.4 129.8 32.6 39 B CYS CB 627 163.1 129.1 33.1 38 B CYS SG 627 163.3 127.7 34.2 39 B CYS C 627 164.2 130.5 31.3 40 B CYS O 627 164.5 130.0 30.2 40 B GLN N 628 163.7 131.7 31.4 40 B GLN CA 628 163.4 132.5 30.3 40 B GLN CB 628 162.5 133.7 30.6 42 B GLN CG 628 161.1 133.4 31.1 44 B GLN CD 628 160.3 134.6 31.5 45 B GLN OE1 628 160.5 135.7 31.0 44 B GLN NE2 628 159.3 134.4 32.4 45 B GLN C 628 164.7 133.0 29.6 40 B GLN O 628 164.7 133.2 28.4 40 B PHE N 629 165.7 133.2 30.4 39 B PHE CA 629 167.0 133.6 29.9 37 B PHE CB 629 168.0 134.1 31.0 37 B PHE CG 629 169.3 134.4 30.6 37 B PHE CD1 629 169.5 135.4 29.6 37 B PHE CD2 629 170.4 133.7 31.0 36 B PHE CE1 629 170.8 135.7 29.1 37 B PHE CE2 629 171.7 133.9 30.5 36 B PHE CZ 629 171.9 134.9 29.5 37 B PHE C 629 167.7 132.5 29.1 37 B PHE O 629 168.2 132.8 28.0 36 B LEU N 630 167.7 131.3 29.6 36 B LEU CA 630 168.2 130.1 29.0 35 B LEU CB 630 168.3 128.9 29.9 33 B LEU CG 630 169.3 129.2 31.1 31 B LEU CD1 630 169.3 128.0 32.0 30 B LEU CD2 630 170.7 129.5 30.6 31 B LEU C 630 167.5 129.8 27.7 36 B LEU O 630 168.1 129.2 26.7 38 B GLU N 631 166.3 130.3 27.5 37 B GLU CA 631 165.5 130.1 26.3 39 B GLU CB 631 164.1 130.4 26.5 43 B GLU CG 631 163.4 129.6 27.6 47 B GLU CD 631 161.9 129.8 27.5 51 B GLU OE1 631 161.3 130.5 28.3 52 B GLU OE2 631 161.2 129.1 26.6 53 B GLU C 631 166.0 131.0 25.2 38 B GLU O 631 165.9 130.7 24.0 37 B LEU N 632 166.6 132.2 25.6 37 B LEU CA 632 167.1 133.1 24.7 36 B LEU CB 632 167.2 134.5 25.4 35 B LEU CG 632 165.9 135.2 25.8 35 B LEU CD1 632 166.3 136.5 26.5 35 B LEU CD2 632 165.0 135.5 24.7 35 B LEU C 632 168.5 132.6 24.2 36 B LEU O 632 168.9 132.9 23.1 36 B CYS N 633 169.2 131.9 25.1 36 B CYS CA 633 170.5 131.4 24.8 35 B CYS CB 633 171.2 130.9 26.1 35 B CYS SG 633 171.5 132.2 27.2 36 B CYS C 633 170.3 130.2 23.8 35 B CYS O 633 171.1 130.0 22.9 36 B GLN N 634 169.2 129.4 24.1 36 B GLN CA 634 168.9 128.2 23.3 35 B GLN CB 634 167.6 127.6 23.7 34 B GLN CG 634 167.2 126.3 23.0 34 B GLN CD 634 166.3 125.4 23.7 34 B GLN OE1 634 165.2 125.8 24.1 35 B GLN NE2 634 166.7 124.2 24.0 33 B GLN C 634 168.8 128.5 21.8 35 B GLN O 634 168.3 129.6 21.4 36 B SER N 635 169.3 127.6 21.0 36 B SER CA 635 169.4 127.8 19.5 36 B SER CB 635 170.7 127.4 19.0 34 B SER OG 635 170.7 127.2 17.6 34 B SER C 635 168.3 127.1 18.8 37 B SER O 635 167.8 126.1 19.2 37 B PRO N 636 167.8 127.6 17.6 38 B PRO CD 636 168.2 129.0 17.1 39 B PRO CA 636 166.8 127.0 16.8 39 B PRO CB 636 166.5 128.1 15.8 40 B PRO CG 636 167.8 128.9 15.7 40 B PRO C 636 167.4 125.8 16.1 40 B PRO O 636 166.8 125.3 15.1 40 B ASP N 637 168.6 125.4 16.4 41 B ASP CA 637 169.2 124.3 15.8 40 B ASP CB 637 170.4 124.8 15.0 43 B ASP CG 637 170.1 125.7 13.9 45 B ASP OD1 637 168.9 125.6 13.3 47 B ASP OD2 637 170.9 126.6 13.5 46 B ASP C 637 169.7 123.4 16.9 39 B ASP O 637 170.5 122.5 16.8 40 B GLY N 638 169.0 123.6 18.1 38 B GLY CA 638 169.3 122.8 19.3 35 B GLY C 638 170.6 123.3 20.0 34 B GLY O 638 171.4 124.0 19.4 36 B GLY N 639 170.7 123.0 21.3 32 B GLY CA 639 171.9 123.4 22.0 30 B GLY C 639 171.7 124.9 22.4 30 B GLY O 639 170.8 125.6 22.0 28 B PHE N 640 172.6 125.3 23.3 29 B PHE CA 640 172.5 126.7 23.8 29 B PHE CB 640 172.3 126.7 25.4 29 B PHE CG 640 171.1 125.9 25.8 29 B PHE CD1 640 171.1 124.5 25.9 29 B PHE CD2 640 170.0 126.6 26.2 29 B PHE CE1 640 170.0 123.8 26.3 29 B PHE CE2 640 168.8 125.9 26.6 29 B PHE CZ 640 168.9 124.5 26.6 29 B PHE C 640 173.8 127.4 23.5 29 B PHE O 640 174.9 126.8 23.4 30 B GLY N 641 173.6 128.7 23.3 27 B GLY CA 641 174.8 129.6 23.0 27 B GLY C 641 175.3 130.1 24.3 27 B GLY O 641 174.8 129.8 25.4 28 B GLY N 642 176.4 130.8 24.3 28 B GLY CA 642 177.0 131.3 25.5 27 B GLY C 642 176.3 132.6 26.0 28 B GLY O 642 176.7 133.2 27.1 28 B GLY N 643 175.2 133.0 25.4 27 B GLY CA 643 174.5 134.2 25.7 27 B GLY C 643 173.4 134.3 24.7 29 B GLY O 643 173.5 133.7 23.6 29 B PRO N 644 172.4 135.2 24.9 29 B PRO CD 644 172.2 136.1 26.0 29 B PRO CA 644 171.3 135.3 23.9 29 B PRO CB 644 170.5 136.5 24.4 28 B PRO CG 644 170.7 136.5 25.9 29 B PRO C 644 171.8 135.6 22.5 31 B PRO O 644 172.6 136.6 22.3 33 B GLY N 645 171.5 134.8 21.6 33 B GLY CA 645 171.9 135.0 20.2 33 B GLY C 645 173.2 134.4 19.7 34 B GLY O 645 173.6 134.5 18.5 35 B GLN N 646 173.9 133.7 20.6 33 B GLN CA 646 175.1 133.0 20.2 32 B GLN CB 646 176.1 133.0 21.4 32 B GLN CG 646 176.5 134.4 21.8 31 B GLN CD 646 177.2 134.5 23.1 31 B GLN OE1 646 176.9 135.4 23.9 31 B GLN NE2 646 178.1 133.5 23.4 30 B GLN C 646 174.9 131.6 19.7 32 B GLN O 646 173.9 131.0 20.0 32 B TYR N 647 175.7 131.2 18.7 31 B TYR CA 647 175.6 129.9 18.1 30 B TYR CB 647 176.8 129.7 17.1 30 B TYR CG 647 176.8 130.7 16.0 30 B TYR CD1 647 177.9 130.8 15.2 31 B TYR CE1 647 177.9 131.6 14.0 31 B TYR CD2 647 175.7 131.4 15.6 30 B TYR CE2 647 175.7 132.2 14.5 30 B TYR CZ 647 176.8 132.3 13.7 31 B TYR OH 647 176.8 133.0 12.6 33 B TYR C 647 175.8 128.9 19.2 30 B TYR O 647 176.5 129.1 20.2 31 B PRO N 648 175.1 127.8 19.1 30 B PRO CD 648 174.2 127.3 18.0 31 B PRO CA 648 175.2 126.7 20.1 29 B PRO CB 648 174.1 125.7 19.7 30 B PRO CG 648 174.2 125.8 18.2 31 B PRO C 648 176.6 126.2 20.3 28 B PRO O 648 177.3 126.0 19.4 29 B HIS N 649 176.9 125.8 21.5 25 B HIS CA 649 178.2 125.3 21.8 23 B HIS CB 649 179.1 126.5 22.2 22 B HIS CG 649 180.5 126.1 22.6 20 B HIS CD2 649 181.7 126.4 21.9 19 B HIS ND1 649 180.9 125.5 23.7 19 B HIS CE1 649 182.2 125.4 23.8 19 B HIS NE2 649 182.7 125.9 22.7 19 B HIS C 649 178.0 124.3 23.0 25 B HIS O 649 177.1 124.6 23.8 26 B LEU N 650 178.7 123.2 23.0 24 B LEU CA 650 178.5 122.2 24.0 24 B LEU CB 650 179.2 120.9 23.7 23 B LEU CG 650 178.6 119.9 22.7 22 B LEU CD1 650 179.6 118.8 22.4 22 B LEU CD2 650 177.3 119.3 23.3 21 B LEU C 650 178.8 122.6 25.5 25 B LEU O 650 178.1 122.1 26.4 26 B ALA N 651 179.7 123.5 25.7 24 B ALA CA 651 180.0 123.9 27.1 24 B ALA CB 651 181.3 124.7 27.2 24 B ALA C 651 178.8 124.7 27.7 25 B ALA O 651 178.3 124.4 28.8 25 B PRO N 652 178.3 125.7 26.9 25 B PRO CD 652 178.9 126.4 25.8 24 B PRO CA 652 177.1 126.4 27.4 25 B PRO CB 652 176.9 127.5 26.4 25 B PRO CG 652 178.3 127.8 25.9 24 B PRO C 652 175.9 125.4 27.5 26 B PRO O 652 175.0 125.6 28.3 28 B THR N 653 175.8 124.5 26.5 26 B THR CA 653 174.7 123.5 26.5 26 B THR CB 653 174.8 122.6 25.3 26 B THR OG1 653 174.7 123.4 24.1 27 B THR CG2 653 173.7 121.7 25.2 26 B THR C 653 174.7 122.6 27.7 26 B THR O 653 173.7 122.3 28.3 27 B TYR N 654 175.9 122.2 28.2 25 B TYR CA 654 175.9 121.3 29.4 24 B TYR CB 654 177.4 120.8 29.5 24 B TYR CG 654 177.7 120.4 30.9 24 B TYR CD1 654 177.4 119.1 31.4 23 B TYR CE1 654 177.8 118.6 32.6 24 B TYR CD2 654 178.4 121.2 31.8 24 B TYR CE2 654 178.8 120.8 33.1 24 B TYR CZ 654 178.5 119.5 33.5 24 B TYR OH 654 178.9 119.0 34.7 25 B TYR C 654 175.5 122.2 30.6 25 B TYR O 654 174.8 121.7 31.4 26 B ALA N 655 176.0 123.4 30.6 26 B ALA CA 655 175.7 124.3 31.7 26 B ALA CB 655 176.5 125.6 31.5 25 B ALA C 655 174.2 124.7 31.7 26 B ALA O 655 173.6 124.7 32.8 26 B ALA N 656 173.6 125.0 30.6 27 B ALA CA 656 172.2 125.3 30.5 29 B ALA CB 656 171.8 125.7 29.2 28 B ALA C 656 171.4 124.1 31.0 31 B ALA O 656 170.6 124.3 31.9 33 B VAL N 657 171.6 123.0 30.4 32 B VAL CA 657 170.9 121.8 30.8 32 B VAL CB 657 171.2 120.6 30.0 32 B VAL CG1 657 170.5 119.4 30.4 32 B VAL CG2 657 170.9 120.8 28.5 30 B VAL C 657 171.0 121.6 32.3 32 B VAL O 657 170.0 121.4 33.0 34 B ASN N 658 172.3 121.6 32.9 32 B ASN CA 658 172.5 121.4 34.3 31 B ASN CB 658 174.0 121.4 34.7 31 B ASN CG 658 174.6 120.1 34.8 31 B ASN OD1 658 174.1 119.1 34.3 33 B ASN ND2 658 175.7 120.0 35.6 32 B ASN C 658 171.7 122.4 35.1 31 B ASN O 658 171.1 122.0 36.1 31 B ALA N 659 171.8 123.6 34.7 31 B ALA CA 659 171.1 124.7 35.4 31 B ALA CB 659 171.3 126.1 34.8 30 B ALA C 659 169.6 124.3 35.5 31 B ALA O 659 169.0 124.2 36.6 31 B LEU N 660 169.0 124.2 34.3 31 B LEU CA 660 167.6 123.8 34.2 31 B LEU CB 660 167.3 123.5 32.7 30 B LEU CG 660 167.3 124.8 31.8 29 B LEU CD1 660 167.1 124.4 30.4 29 B LEU CD2 660 166.2 125.7 32.3 29 B LEU C 660 167.2 122.7 35.0 33 B LEU O 660 166.1 122.6 35.6 35 B CYS N 661 168.1 121.7 35.3 35 B CYS CA 661 167.8 120.5 36.1 36 B CYS CB 661 168.7 119.4 35.7 35 B CYS SG 661 168.3 118.6 34.2 34 B CYS C 661 167.9 120.8 37.6 37 B CYS O 661 167.2 120.2 38.4 37 B ILE N 662 168.7 121.8 38.0 38 B ILE CA 662 168.9 122.2 39.4 39 B ILE CB 662 170.1 123.1 39.6 38 B ILE CG2 662 170.2 123.4 41.1 39 B ILE CG1 662 171.4 122.4 39.2 38 B ILE CD1 662 172.6 123.2 39.5 37 B ILE C 662 167.5 122.8 39.8 39 B ILE O 662 167.0 122.6 40.9 40 B ILE N 663 167.0 123.6 38.9 39 B ILE CA 663 165.7 124.3 39.1 39 B ILE CB 663 165.5 125.3 38.0 37 B ILE CG2 663 164.1 125.9 38.0 37 B ILE CG1 663 166.5 126.5 38.2 36 B ILE CD1 663 166.6 127.4 37.0 34 B ILE C 663 164.6 123.2 39.0 41 B ILE O 663 163.6 123.3 39.7 42 B GLY N 664 164.9 122.1 38.3 41 B GLY CA 664 163.9 121.0 36.2 42 B GLY C 664 162.4 121.2 38.2 42 B GLY O 664 161.7 120.4 38.8 44 B THR N 665 161.9 122.2 37.5 42 B THR CA 665 160.5 122.4 37.4 42 B THR CB 665 160.1 123.9 37.6 41 B THR OG1 665 160.3 124.6 36.4 41 B THR CG2 665 160.9 124.5 38.7 41 B THR C 665 160.0 122.0 36.1 43 B THR O 665 160.8 121.8 35.1 43 B GLU N 666 158.7 121.8 35.9 45 B GLU CA 666 158.2 121.4 34.6 47 B GLU CB 666 156.7 120.9 34.7 49 B GLU CG 666 156.6 119.3 35.0 51 B GLU CD 666 157.4 118.9 36.3 53 B GLU OE1 666 157.5 119.6 37.3 54 B GLU OE2 666 157.9 117.7 36.3 53 B GLU C 666 158.3 122.5 33.7 47 B GLU O 666 158.1 122.3 32.5 48 B GLU N 667 158.7 123.7 34.2 46 B GLU CA 667 158.9 124.8 33.3 46 B GLU CB 667 158.7 126.1 34.1 48 B GLU CG 667 158.8 127.4 33.3 49 B GLU CD 667 159.2 128.6 34.1 50 B GLU OE1 667 159.2 128.5 35.3 49 B GLU OE2 667 159.5 129.6 33.4 51 B GLU C 667 160.4 124.8 32.8 45 B GLU O 667 160.6 125.1 31.7 45 B ALA N 668 161.3 124.5 33.7 42 B ALA CA 668 162.7 124.4 33.4 40 B ALA CB 668 163.5 124.1 34.6 40 B ALA C 668 162.8 123.3 32.3 39 B ALA O 668 163.2 123.5 31.2 38 B TYR N 669 162.4 122.1 32.7 38 B TYR CA 669 162.5 120.9 31.8 36 B TYR CB 669 161.7 119.7 32.4 34 B TYR CG 669 162.2 119.2 33.7 32 B TYR CD1 669 161.3 118.8 34.7 32 B TYR CE1 669 161.8 118.2 35.9 30 B TYR CD2 669 163.6 119.1 34.0 31 B TYR CE2 669 164.0 118.6 35.3 30 B TYR CZ 669 163.1 118.2 36.2 29 B TYR OH 669 163.5 117.7 37.4 28 B TYR C 669 161.9 121.2 30.5 37 B TYR O 669 162.5 120.9 29.4 38 B ASN N 670 160.8 121.9 30.5 37 B ASN CA 670 160.2 122.3 29.2 38 B ASN CB 670 158.7 122.7 29.4 39 B ASN CG 670 157.8 121.5 29.6 39 B ASN OD1 670 158.0 120.6 30.4 39 B ASN ND2 670 156.7 121.5 28.8 40 B ASN C 670 160.9 123.2 28.3 38 B ASN O 670 160.5 123.5 27.2 39 B VAL N 671 161.9 123.8 28.8 37 B VAL CA 671 162.7 124.8 28.0 37 B VAL CB 671 163.8 125.5 28.9 37 B VAL CG1 671 164.7 126.3 28.0 37 B VAL CG2 671 163.1 126.4 29.9 37 B VAL C 671 163.5 124.0 26.9 37 B VAL O 671 163.4 124.4 25.7 37 B ILE N 672 164.1 122.9 27.3 37 B ILE CA 672 164.9 122.1 26.4 36 B ILE CB 672 165.6 121.0 27.2 34 B ILE CG2 672 166.7 120.3 26.3 34 B ILE CG1 672 166.3 121.5 28.5 34 B ILE CD1 672 166.8 120.5 29.4 33 B ILE C 672 164.2 121.5 25.3 37 B ILE O 672 163.3 120.7 25.5 38 B ASN N 673 164.6 121.8 24.0 38 B ASN CA 673 164.0 121.2 22.8 39 B ASN CB 673 164.1 122.2 21.7 40 B ASN CG 673 163.6 121.7 20.4 42 B ASN OD1 673 163.8 120.5 20.0 43 B ASN ND2 673 162.8 122.5 19.6 42 B ASN C 673 164.8 119.9 22.5 40 B ASN O 673 165.8 120.0 21.8 40 B ARG N 674 164.3 118.8 23.0 40 B ARG CA 674 165.0 117.5 22.8 39 B ARG CB 674 164.3 116.5 23.7 38 B ARG CG 674 164.2 116.9 25.1 38 B ARG CD 674 163.2 116.0 25.9 40 B ARG NE 674 163.6 114.5 25.8 41 B ARG CZ 674 163.1 113.6 25.0 41 B ARG NH1 674 162.1 113.9 24.1 41 B ARG NH2 674 163.5 112.4 25.0 42 B ARG C 674 165.2 117.0 21.4 40 B ARG O 674 166.1 116.4 21.1 40 B GLU N 675 164.2 117.3 20.5 41 B GLU CA 675 164.4 116.7 19.1 43 B GLU CB 675 163.1 116.9 18.3 46 B GLU CG 675 162.1 117.9 18.9 51 B GLU CD 675 161.3 117.5 20.2 53 B GLU OE1 675 161.5 118.2 21.2 53 B GLU OE2 675 160.6 116.5 20.2 54 B GLU C 675 165.5 117.5 18.4 42 B GLU O 675 166.3 116.9 17.7 41 B LYS N 676 165.6 118.8 18.7 41 B LYS CA 676 166.6 119.6 18.1 40 B LYS CB 676 166.2 121.0 17.9 41 B LYS CG 676 165.7 121.2 16.5 43 B LYS CD 676 165.6 122.7 16.2 46 B LYS CE 676 164.6 123.4 17.0 48 B LYS NZ 676 164.3 124.9 16.6 49 B LYS C 676 167.9 119.5 18.9 37 B LYS O 676 169.0 119.6 18.3 37 B LEU N 677 167.9 119.2 20.2 36 B LEU CA 677 169.1 119.0 20.9 34 B LEU CB 677 168.8 118.7 22.4 33 B LEU CG 677 170.0 118.4 23.3 32 B LEU CD1 677 171.1 119.4 23.1 32 B LEU CD2 677 169.6 118.3 24.7 31 B LEU C 677 169.9 117.8 20.3 35 B LEU O 677 171.1 117.9 20.1 36 B LEU N 678 169.2 116.7 20.0 36 B LEU CA 678 169.7 115.5 19.4 37 B LEU CB 678 168.6 114.5 19.2 37 B LEU CG 678 168.9 113.0 19.2 38 B LEU CD1 678 167.9 112.3 18.3 37 B LEU CD2 678 170.3 112.7 18.8 38 B LEU C 678 170.3 115.9 18.1 37 B LEU O 678 171.4 115.5 17.7 37 B GLN N 679 169.5 116.6 17.3 37 B GLN CA 679 169.9 117.0 16.0 38 B GLN CB 679 168.9 118.0 15.4 41 B GLN CG 679 169.1 118.5 14.0 44 B GLN CD 679 167.9 119.2 13.4 46 B GLN OE1 679 167.9 120.4 13.2 48 B GLN NE2 679 166.8 118.4 13.3 47 B GLN C 679 171.3 117.6 16.0 37 B GLN O 679 172.2 117.3 15.3 37 B TYR N 680 171.4 118.5 17.0 34 B TYR CA 680 172.7 119.3 17.3 31 B TYR CB 680 172.5 120.3 18.4 31 B TYR CG 680 173.7 121.1 18.7 29 B TYR CD1 680 174.3 121.9 17.8 29 B TYR CE1 680 175.4 122.6 18.1 28 B TYR CD2 680 174.3 121.1 20.0 28 B TYR CE2 680 175.4 121.8 20.3 27 B TYR CZ 680 175.9 122.6 19.3 27 B TYR OH 680 177.0 123.3 19.7 28 B TYR C 680 173.8 118.3 17.6 30 B TYR O 680 174.8 118.2 17.0 29 B LEU N 681 173.6 117.4 18.6 28 B LEU CA 681 174.6 116.5 19.0 29 B LEU CB 681 174.1 115.6 20.2 28 B LEU CG 681 173.7 116.2 21.5 27 B LEU CD1 681 173.3 115.2 22.5 26 B LEU CD2 681 174.9 117.0 22.0 27 B LEU C 681 175.1 115.6 17.8 29 B LEU O 681 176.2 115.3 17.7 29 B TYR N 682 174.1 115.4 16.9 30 B TYR CA 682 174.5 114.6 15.7 31 B TYR CB 682 173.2 114.1 15.0 32 B TYR CG 682 172.8 112.7 15.3 32 B TYR CD1 682 171.5 112.4 15.6 32 B TYR CE1 682 171.1 111.1 15.9 32 B TYR CD2 682 173.8 111.7 15.3 33 B TYR CE2 682 173.4 110.4 15.6 33 B TYR CZ 682 172.1 110.1 15.9 33 B TYR OH 682 171.7 108.8 16.2 33 B TYR C 682 175.3 115.5 14.8 32 B TYR O 682 176.2 115.0 14.1 32 B SER N 683 175.1 116.8 14.8 32 F SER CA 683 175.9 117.7 14.0 31 B SER CB 683 175.2 119.1 13.9 30 B SER OG 683 175.4 119.8 15.2 28 B SER C 683 177.3 117.8 14.4 32 B SER O 683 178.2 118.3 13.7 33 B LEU N 684 177.6 117.3 15.6 30 B LEU CA 684 179.0 117.4 16.1 29 B LEU CB 684 178.9 118.0 17.5 27 B LEU CG 684 178.2 119.3 17.7 25 B LEU CD1 684 178.1 119.7 19.1 24 B LEU CD2 684 178.8 120.4 16.8 25 B LEU C 684 179.8 116.1 16.1 29 B LEU O 684 181.0 116.1 16.0 30 B LYS N 685 179.0 115.0 16.1 28 B LYS CA 685 179.7 113.7 16.1 27 B LYS CB 685 178.6 112.6 15.9 27 B LYS CG 685 178.7 111.4 16.8 27 B LYS CD 685 180.1 110.8 16.9 27 B LYS CE 685 180.1 109.6 17.7 27 B LYS NZ 685 179.3 108.4 17.1 27 B LYS C 685 180.7 113.6 15.0 27 B LYS O 685 180.5 114.2 13.9 26 B GLN N 686 181.8 112.9 15.2 27 B GLN CA 686 182.8 112.7 14.2 27 B GLN CB 686 184.1 113.3 14.8 27 B GLN CG 686 184.1 114.7 15.0 28 B GLN CD 686 183.9 115.5 13.8 29 B GLN OE1 686 184.7 115.6 12.9 31 B GLN NE2 686 182.7 116.1 13.7 30 B GLN C 686 183.0 111.2 14.0 28 B GLN O 686 182.5 110.4 14.8 29 B PRO N 687 183.5 110.8 12.9 29 B PRO CD 687 183.9 111.7 11.7 30 B PRO CA 687 183.7 109.4 12.6 29 B PRO CB 687 184.4 109.5 11.2 29 B PRO CG 687 183.8 110.6 10.6 30 B PRO C 687 184.6 108.7 13.6 30 B PRO O 687 184.4 107.5 13.8 31 B ASP N 688 185.6 109.4 14.2 29 B ASP CA 688 186.4 108.7 15.1 28 B ASP CB 688 187.8 109.3 15.2 28 B ASP CG 688 187.9 110.7 15.7 29 B ASP OD1 688 186.8 111.3 15.9 30 B ASP OD2 688 189.0 111.2 15.9 30 B ASP C 688 185.8 108.6 16.5 27 B ASP O 688 186.4 108.1 17.4 29 B GLY N 689 184.5 109.1 16.6 25 B GLY CA 689 183.9 109.0 17.9 24 B GLY C 689 183.8 110.3 18.7 24 B GLY O 689 183.0 110.4 19.6 25 B SER N 690 184.6 111.2 18.3 22 B SER CA 690 184.7 112.5 19.0 21 B SER CB 690 186.0 113.2 18.8 20 B SER OG 690 186.2 113.3 17.4 20 B SER C 690 183.s 113.4 18.6 21 B SER O 690 182.7 113.0 17.7 23 B PHE N 691 183.4 114.5 19.2 21 B PHE CA 691 182.4 115.5 18.9 20 B PHE CB 691 181.4 115.6 20.0 19 B PHE CG 691 180.5 114.5 20.2 19 B PHE CD1 691 180.8 113.4 20.9 18 B PHE CD2 691 179.2 114.5 19.6 19 B PHE CE1 691 180.0 112.3 21.1 18 B PHE CE2 691 178.3 113.4 19.8 19 B PHE CZ 691 178.7 112.3 20.5 18 B PHE C 691 183.1 116.9 18.8 21 B PHE O 691 184.1 117.1 19.5 20 B LEU N 692 182.6 117.8 18.0 21 B LEU CA 692 183.2 119.1 18.0 22 B LEU CB 692 182.8 119.9 16.7 21 B LEU CG 692 183.0 119.2 15.4 21 B LEU CD1 692 182.3 120.0 14.4 20 B LEU CD2 692 184.5 119.0 15.1 19 B LEU C 692 182.6 119.8 19.2 23 B LEU O 692 181.6 119.4 19.7 24 B MET N 693 183.2 120.9 19.7 24 B MET CA 693 182.6 121.7 20.8 22 B MET CB 693 183.7 122.5 21.5 21 B MET CG 693 184.7 121.8 22.3 21 B MET SD 693 184.0 120.8 23.7 23 B MET CE 693 183.2 122.1 24.7 21 B MET C 693 181.5 122.5 20.2 21 B MET O 693 180.5 122.9 20.9 22 B HIS N 694 181.6 122.8 19.0 22 B HIS CA 694 180.6 123.6 18.2 23 B HIS CB 694 180.5 125.0 18.7 23 B HIS CG 694 181.8 125.8 18.5 23 B HIS CD2 694 183.0 125.7 19.1 23 B HIS ND1 694 181.9 126.8 17.5 23 B HIS CE1 694 183.1 127.3 17.6 23 B HIS NE2 694 183.8 126.7 18.5 23 B HIS C 694 181.0 123.5 16.7 25 B HIS O 694 182.0 122.9 16.3 26 B VAL N 695 180.1 123.9 15.8 25 B VAL CA 695 180.3 123.8 14.4 25 B VAL CB 695 179.0 124.3 13.7 26 B VAL CG1 695 179.3 124.5 12.2 27 B VAL CG2 695 177.9 123.2 13.8 25 B VAL C 695 181.5 124.7 14.0 26 B VAL O 695 181.5 125.9 14.3 28 B GLY N 696 182.4 124.1 13.4 25 B GLY CA 696 183.6 124.9 13.0 25 B GLY C 696 184.6 125.0 14.2 25 B GLY O 696 185.6 125.6 14.0 25 B GLY N 697 184.2 124.3 15.3 24 B GLY CA 697 185.1 124.4 16.5 23 B GLY C 697 186.1 123.3 16.7 23 B GLY O 697 186.2 122.3 15.9 23 B GLU N 698 186.7 123.4 17.8 22 B GLU CA 698 187.7 122.4 18.3 22 B GLU CB 698 188.6 123.1 19.3 21 B GLU CG 698 188.1 123.3 20.7 22 B GLU CD 698 187.2 124.5 20.9 23 B GLU OE1 698 186.9 125.2 19.9 23 B GLU OE2 698 186.8 124.7 22.1 24 B GLU C 698 187.1 121.1 18.8 21 B GLU O 698 186.0 121.0 19.2 22 B VAL N 699 188.0 120.1 18.9 21 B VAL CA 699 187.6 118.8 19.5 20 B VAL CB 699 187.7 117.6 18.4 20 B VAL CG1 699 187.7 116.3 19.1 20 B VAL CG2 699 186.7 117.7 17.4 21 B VAL C 699 188.5 118.3 20.6 21 B VAL O 699 189.7 118.3 20.5 22 B ASP N 700 187.9 118.0 21.8 21 B ASP CA 700 188.7 117.5 22.9 22 B ASP CB 700 189.6 118.6 23.6 24 B ASP CG 700 188.8 119.7 24.2 27 B ASP OD1 700 187.9 119.4 25.0 27 B ASP OD2 700 189.1 120.9 23.9 28 B ASP C 700 187.7 116.8 23.8 22 B ASP O 700 186.5 116.9 23.6 22 B VAL N 701 188.1 116.1 24.9 22 B VAL CA 701 187.2 115.4 25.8 21 B VAL CB 701 187.9 114.6 26.9 20 B VAL CG1 701 187.6 113.1 26.8 20 B VAL CG2 701 189.3 114.9 27.0 22 B VAL C 701 186.0 116.1 26.4 22 B VAL O 701 185.0 115.5 26.7 23 B ARG N 702 186.1 117.4 26.5 22 B ARG CA 702 185.0 118.1 27.1 23 B ARG CB 702 185.3 119.6 27.2 23 B ARG CG 702 186.5 120.1 28.0 22 B ARG CD 702 186.8 121.5 27.7 23 B ARG NE 702 187.2 121.8 26.3 24 B ARG CZ 702 186.9 122.8 25.6 24 B ARG NH1 702 187.3 122.9 24.3 24 B ARG NH2 702 186.3 123.8 26.2 25 B ARG C 702 183.7 117.8 26.4 25 B ARG O 702 182.7 117.5 27.0 26 B SER N 703 183.8 117.7 25.1 26 B SER CA 703 182.6 117.5 24.2 26 B SER CB 703 183.0 117.6 22.7 26 B SER OG 703 183.9 116.7 22.3 27 B SER C 703 182.0 116.1 24.4 27 B SER O 703 180.7 116.0 24.4 28 B ALA N 704 182.8 115.1 24.7 27 B ALA CA 704 182.3 113.7 24.9 27 B ALA CB 704 183.5 112.8 25.1 27 B ALA C 704 181.5 113.7 26.2 27 B ALA O 704 180.5 113.0 26.3 28 B TYR N 705 181.9 114.5 27.2 28 B TYR CA 705 181.2 114.6 28.5 27 B TYR CB 705 182.2 115.1 29.6 27 B TYR CG 705 181.6 115.5 30.9 27 B TYR CD1 705 180.9 114.5 31.6 27 B TYR CE1 705 180.4 114.8 32.9 27 B TYR CD2 705 181.6 116.8 31.4 26 B TYR CE2 705 181.1 117.1 32.6 27 B TYR CZ 705 180.4 116.1 33.3 26 B TYR OH 705 179.9 116.4 34.5 27 B TYR C 705 180.0 115.5 28.4 26 B TYR O 705 178.9 115.2 29.0 25 B CYS N 706 180.2 116.7 27.8 25 B CYS CA 706 179.1 117.6 27.7 25 B CYS CB 706 179.5 118.8 26.9 25 B CYS SG 706 180.7 119.8 27.9 24 B CYS C 706 177.9 116.9 27.0 26 B CYS O 706 176.8 116.9 27.4 27 B ALA N 707 178.2 116.2 25.9 26 B ALA CA 707 177.2 115.4 25.1 24 B ALA CB 707 177.9 114.9 23.8 24 B ALA C 707 176.6 114.3 25.9 24 B ALA O 707 175.4 114.2 25.9 24 B ALA N 708 177.4 113.5 26.5 25 B ALA CA 708 176.9 112.3 27.3 25 B ALA CB 708 178.0 111.4 27.7 24 B ALA C 708 176.0 112.8 28.5 27 B ALA O 708 175.2 112.0 28.9 28 B SER N 709 176.3 113.9 29.0 28 B SER CA 709 175.6 114.5 30.2 29 B SER CB 709 176.4 115.6 30.9 29 B SER OG 709 175.7 116.0 32.1 30 B SER C 709 174.2 115.0 29.8 29 B SER O 709 173.2 114.7 30.4 30 B VAL N 710 174.1 115.8 28.7 30 B VAL CA 710 172.9 116.3 28.2 30 B VAL CB 710 173.1 117.5 27.3 31 B VAL CG1 710 174.0 118.5 28.0 31 B VAL CG2 710 173.6 117.1 25.9 31 B VAL C 710 172.0 115.2 27.6 30 B VAL O 710 170.8 115.1 27.9 30 B ALA N 711 172.6 114.4 26.7 30 B ALA CA 711 171.8 113.4 26.0 30 B ALA CB 711 172.7 112.6 25.0 28 B ALA C 711 171.2 112.4 27.0 30 B ALA O 711 170.1 111.9 26.8 30 B SER N 712 172.0 112.0 28.0 31 B SER CA 712 171.5 111.1 29.0 31 B SER CB 712 172.6 110.5 29.8 31 B SER OG 712 173.3 111.4 30.7 31 B SER C 712 170.4 111.7 29.9 31 B SER O 712 169.3 111.1 30.0 31 B LEU N 713 170.7 112.8 30.6 30 B LEU CA 713 169.7 113.4 31.4 30 B LEU CB 713 170.2 114.8 32.0 29 B LEU CG 713 171.2 114.8 33.1 29 B LEU CD1 713 171.7 116.3 33.3 28 B LEU CD2 713 170.7 114.3 34.4 28 B LEU C 713 168.4 113.7 30.7 32 B LEU O 713 167.3 113.5 31.3 32 B THR N 714 168.4 114.0 29.4 33 B THR CA 714 167.2 114.3 28.7 33 B THR CB 714 167.4 115.5 27.7 34 B THR OG1 714 168.6 115.2 26.8 34 B THR CG2 714 167.7 116.8 28.4 33 B THR C 714 166.7 113.1 27.9 34 B THR O 714 165.6 113.2 27.3 35 B ASN N 715 167.3 111.9 28.0 34 B ASN CA 715 166.9 110.7 27.4 33 B ASN CB 715 165.5 110.3 28.0 34 B ASN CG 715 164.8 109.1 27.4 35 B ASN OD1 715 165.5 108.1 27.0 36 B ASN ND2 715 163.5 109.1 27.3 36 B ASN C 715 166.8 110.8 25.9 32 B ASN O 715 165.7 110.6 25.3 34 B ILE N 716 167.9 111.2 25.2 31 B ILE CA 716 167.8 111.3 23.7 30 B ILE CB 716 168.1 112.7 23.2 30 B ILE CG2 716 166.9 113.6 23.6 30 B ILE CG1 716 169.4 113.3 23.8 31 B ILE CD1 716 169.8 114.6 23.3 30 B ILE C 716 168.9 110.5 23.2 30 B ILE O 716 169.3 110.7 22.0 30 B ILE N 717 169.4 109.5 24.0 30 B ILE CA 717 170.4 108.6 23.5 32 B ILE CB 717 171.2 108.0 24.7 32 B ILE CG2 717 172.2 107.0 24.2 31 B ILE CG1 717 171.8 109.0 25.6 31 B ILE CD1 717 172.8 108.5 26.6 31 B ILE C 717 169.9 107.6 22.5 33 B ILE O 717 169.2 106.6 22.9 34 B THR N 718 170.1 107.8 21.2 34 B THR CA 718 169.8 106.9 20.2 35 B THR CB 718 169.8 107.6 18.8 35 B THR OG1 718 171.1 107.9 18.5 35 B THR CG2 718 169.0 108.8 18.8 35 B THR C 718 170.8 105.8 20.3 37 B THR O 718 171.7 105.8 21.0 38 B PRO N 719 170.6 104.7 19.4 39 B PRO CD 719 169.5 104.5 18.6 39 B PRO CA 719 171.6 103.6 19.4 39 B PRO CB 719 170.9 102.7 18.4 40 B PRO CG 719 169.4 103.0 18.5 40 B PRO C 719 173.0 103.8 18.9 38 B PRO O 719 173.9 103.2 19.4 37 B ASP N 720 173.1 104.7 17.9 38 B ASP CA 720 174.5 105.0 17.4 39 B ASP CB 720 174.4 104.9 15.9 40 B ASP CG 720 173.5 105.9 15.2 41 B ASP OD1 720 173.9 106.3 14.1 42 B ASP OD2 720 172.5 106.3 15.9 42 B ASP C 720 175.0 106.4 17.7 38 B ASP O 720 176.0 106.8 17.2 38 B LEU N 721 174.3 107.2 18.6 37 B LEU CA 721 174.8 108.5 18.9 36 B LEU CB 721 173.9 109.1 20.0 35 B LEU CG 721 174.3 110.5 20.4 34 B LEU CD1 721 174.6 111.4 19.2 33 B LEU CD2 721 173.3 111.1 21.3 33 B LEU C 721 176.2 108.5 19.4 36 B LEU O 721 177.1 109.2 18.9 37 B PHE N 722 176.5 107.6 20.4 36 B PHE CA 722 177.8 107.6 21.0 36 B PHE CB 722 177.6 107.5 22.6 36 B PHE CG 722 177.0 108.8 23.1 36 B PHE CD1 722 175.7 108.8 23.6 35 B PHE CD2 722 177.7 110.0 23.0 35 B PHE CE1 722 175.2 109.9 24.1 35 B PHE CE2 722 177.1 111.1 23.5 35 B PHE CZ 722 175.8 111.1 24.0 35 B PHE C 722 178.6 106.4 20.6 37 B PHE O 722 179.4 105.8 21.3 38 B GLU N 723 178.4 106.1 19.3 38 B GLU CA 723 179.2 105.0 18.7 37 B GLU CB 723 178.7 104.7 17.3 41 B GLU CG 723 178.8 103.2 17.0 45 B GLU CD 723 178.1 102.4 18.0 47 B GLU OE1 723 176.8 102.4 18.0 49 B GLU OE2 723 178.8 101.9 18.9 48 B GLU C 723 180.6 105.4 18.6 34 B GLU O 723 181.0 106.4 18.0 33 B GLY N 724 181.5 104.5 19.2 32 B GLY CA 724 182.9 104.8 19.2 31 B GLY C 724 183.4 105.9 20.1 30 B GLY O 724 184.6 106.0 20.2 30 B THR N 725 182.6 106.6 20.8 29 B THR CA 725 183.1 107.6 21.7 29 B THR CB 725 182.1 108.8 21.9 28 B THR OG1 725 181.9 109.0 23.3 30 B THR CG2 725 180.9 108.7 21.1 26 B THR C 725 183.8 107.1 22.9 28 B THR O 725 184.7 107.6 23.4 28 B ALA N 726 183.4 105.9 23.3 27 B ALA CA 726 184.0 105.3 24.5 26 B ALA CB 726 183.2 104.1 24.9 26 B ALA C 726 185.4 104.9 24.1 27 B ALA O 726 186.4 105.0 24.8 28 B GLU N 727 185.5 104.5 22.8 27 B GLU CA 727 186.8 104.0 22.2 27 B GLU CB 727 186.6 103.3 20.9 28 B GLU CG 727 186.1 101.8 21.1 28 B GLU CD 727 184.6 101.6 21.4 29 B GLU OE1 727 184.3 100.5 21.8 31 B GLU OE2 727 183.8 102.6 21.2 30 B GLU C 727 187.8 105.2 22.1 26 B GLU O 727 189.0 105.1 22.4 26 B TRP N 728 187.2 106.3 21.5 24 B TRP CA 728 188.1 107.5 21.3 23 B TRP CB 728 187.3 108.6 20.6 22 B TRP CG 728 188.1 109.8 20.3 20 B TRP CD2 728 188.2 110.9 21.1 20 B TRP CE2 728 189.1 111.8 20.4 20 B TRP CE3 728 187.7 111.3 22.3 20 B TRP CD1 728 188.9 109.9 19.2 20 B TRP NE1 728 189.5 111.2 19.3 20 B TRP C22 728 189.5 113.0 20.9 20 B TRP CZ3 728 188.0 112.6 22.8 19 B TRP CH2 728 188.9 113.4 22.1 20 B TRP C 728 188.6 108.0 22.7 24 B TRP O 728 189.8 108.2 22.8 25 B ILE N 729 187.7 108.1 23.7 24 B ILE CA 729 188.0 108.6 25.0 23 B ILE CB 729 186.8 108.6 25.9 23 B ILE CG2 729 187.3 108.9 27.4 23 B ILE CG1 729 185.8 109.6 25.5 23 B ILE CD1 729 184.4 109.5 26.1 22 B ILE C 729 189.1 107.7 25.6 24 B ILE O 729 190.1 108.2 26.1 24 B ALA N 730 189.0 106.4 25.4 23 B ALA CA 730 190.0 105.5 25.9 23 B ALA CB 730 189.5 104.0 25.6 23 B ALA C 730 191.4 105.8 25.3 24 B ALA O 730 192.4 105.4 25.8 25 B ARG N 731 191.4 106.5 24.2 25 B ARG CA 731 192.7 106.8 23.5 25 B ARG CB 731 192.4 107.1 22.0 26 B ARG CG 731 192.0 105.8 21.2 27 B ARG CD 731 192.5 105.9 19.8 27 B ARG NE 731 191.8 106.8 19.0 28 B ARG CZ 731 192.3 107.8 18.3 30 B ARG NH1 731 193.6 107.9 18.2 28 B ARG NH2 731 191.5 108.6 17.5 30 B ARG C 731 193.3 108.0 24.1 26 B ARG O 731 194.5 108.3 23.8 26 B CYS N 732 192.6 108.8 24.9 26 B CYS CA 732 193.1 110.0 25.5 24 B CYS CB 732 191.9 110.9 25.9 24 B CYS SG 732 191.1 111.4 24.4 24 B CYS C 732 193.9 109.6 26.8 24 B CYS O 732 194.6 110.4 27.3 24 B GLN N 733 193.7 108.3 27.2 24 B GLN CA 733 194.5 107.9 28.4 24 B GLN CB 733 193.9 106.6 29.0 23 B GLN CG 733 194.6 106.1 30.3 23 B GLN CD 733 193.9 104.9 31.0 22 B GLN OE1 733 193.2 104.1 30.3 23 B GLN NE2 733 194.1 104.8 32.3 22 B GLN C 733 196.0 107.6 28.0 24 B GLN O 733 196.2 106.8 27.0 24 B ASN N 734 196.9 108.2 28.6 24 B ASN CA 734 198.3 108.1 28.3 23 B ASN CB 734 198.9 109.5 28.1 23 B ASN CG 734 199.2 110.2 29.4 22 B ASN OD1 734 198.9 109.7 30.5 21 B ASN ND2 734 200.0 111.3 29.4 21 B ASN C 734 199.2 107.3 29.2 22 B ASN O 734 198.7 106.7 30.2 23 B TRP N 735 200.5 107.3 29.0 22 B TRP CA 735 201.5 106.6 29.8 23 B TRP CB 735 202.8 106.9 29.3 21 B TRP CG 735 203.2 108.4 29.3 21 B TRP CD2 735 203.9 109.1 30.2 21 B TRP CE2 735 204.0 110.4 29.8 22 B TRP CE3 735 204.5 108.8 31.5 21 B TRP CD1 735 202.8 109.2 28.3 22 B TRP NE1 735 203.3 110.5 28.6 22 B TRP CZ2 735 204.6 111.5 30.5 21 B TRP CZ3 735 205.1 109.8 32.2 21 B TRP CH2 735 205.2 111.1 31.7 21 B TRP C 735 201.4 107.0 31.3 25 B TRP O 735 201.9 106.2 32.2 26 B GLU N 736 200.8 108.1 31.7 25 B GLU CA 736 200.7 108.6 33.0 24 B GLU CB 736 200.5 110.1 33.1 23 B GLU CG 736 201.5 111.0 32.4 23 B GLU CD 736 201.2 112.5 32.5 24 B GLU OE1 736 200.9 113.1 31.5 23 B GLU OE2 736 201.3 113.0 33.7 23 B GLU C 736 199.6 108.0 33.9 24 B GLU O 736 199.6 108.1 35.1 27 B GLY N 737 196.6 107.5 33.2 22 B GLY CA 737 197.5 106.9 33.9 18 B GLY C 737 196.3 107.9 33.8 18 B GLY O 737 195.2 107.5 33.9 18 B GLY N 738 196.7 109.1 33.5 17 B GLY CA 738 195.6 110.1 33.4 17 B GLY C 738 195.0 110.2 32.0 17 B GLY O 738 195.3 109.3 31.1 17 B ILE N 739 194.2 111.2 31.7 16 B ILE CA 739 193.6 111.3 30.4 15 B ILE CB 739 192.1 111.1 30.5 14 B ILE CG2 739 191.4 111.6 29.3 13 B ILE CG1 739 191.8 109.6 30.8 14 B ILE CD1 739 190.3 109.3 30.9 13 B ILE C 739 193.9 112.7 29.9 16 B ILE O 739 193.8 113.7 30.6 17 B GLY N 740 194.3 112.8 28.6 16 B GLY CA 740 194.6 114.1 28.0 15 B GLY C 740 193.4 114.7 27.3 14 B GLY O 740 192.3 114.1 27.3 14 B GLY N 741 193.5 115.9 26.8 16 B GLY CA 741 192.4 116.5 26.0 18 B GLY C 741 192.1 115.8 24.7 18 B GLY O 741 190.9 115.8 24.3 20 B VAL N 742 193.1 115.3 24.1 19 B VAL CA 742 193.0 114.5 22.8 18 B VAL CB 742 193.3 115.4 21.6 17 B VAL CG1 742 192.2 116.4 21.4 16 B VAL CG2 742 194.7 116.0 21.7 17 B VAL C 742 194.2 113.5 23.0 19 B VAL O 742 195.1 113.7 23.8 20 B PRO N 743 194.1 112.4 22.2 20 B PRO CD 743 193.1 111.9 21.3 19 B PRO CA 743 195.2 111.4 22.2 19 B PRO CB 743 194.9 110.4 21.1 18 B PRO CG 743 193.4 110.4 21.2 18 B PRO C 743 196.6 111.9 22.1 20 B PRO O 743 196.9 112.8 21.3 21 B GLY N 744 197.5 111.5 23.0 20 B GLY CA 744 198.9 112.0 22.9 20 B GLY C 744 199.2 113.1 23.9 21 B GLY O 744 200.4 113.3 24.1 20 B MET N 745 198.2 113.8 24.4 21 B MET CA 745 198.3 114.9 25.3 21 B MET CB 745 197.2 115.9 25.1 20 B MET CG 745 197.5 117.0 24.1 20 B MET SD 745 199.1 117.6 24.3 20 B MET CE 745 198.8 118.9 25.3 21 B MET C 745 198.6 114.6 26.8 21 B MET O 745 198.2 113.5 27.2 22 B GLU N 746 199.2 115.5 27.4 22 B GLU CA 746 199.5 115.3 28.8 23 B GLU CB 746 200.3 116.5 29.4 23 B GLU CG 746 200.7 116.4 30.8 25 B GLU CD 746 201.3 117.7 31.3 27 B GLU OE1 746 201.1 118.7 30.7 28 B GLU OE2 746 201.9 117.6 32.4 27 B GLU C 746 198.3 115.1 29.7 24 B GLU O 746 197.3 115.8 29.4 25 B ALA N 747 198.3 114.1 30.6 23 B ALA CA 747 197.2 113.9 31.5 23 B ALA CB 747 197.4 112.7 32.4 23 B ALA C 747 196.8 115.1 32.3 23 B ALA O 747 197.7 115.6 32.9 23 B HIS N 748 195.5 115.4 32.3 22 B HIS CA 748 195.1 116.6 33.1 22 B HIS CB 748 194.9 117.8 32.1 21 B HIS CG 748 194.8 119.1 32.7 21 B HIS CD2 748 195.7 120.0 32.9 20 B HIS ND1 748 193.7 119.6 33.4 21 B HIS CE1 748 193.9 120.7 33.9 20 B HIS NE2 748 195.2 121.0 33.7 20 B HIS C 748 193.8 116.3 33.9 23 B HIS O 748 193.0 115.4 33.5 24 B GLY N 749 193.6 117.0 35.0 23 B GLY CA 749 192.4 116.8 35.8 21 B GLY C 749 191.0 117.1 35.2 21 B GLY O 749 190.1 116.3 35.4 23 B GLY N 750 190.9 118.3 34.6 21 B GLY CA 750 189.6 118.6 34.0 20 B GLY C 750 189.2 117.6 32.9 20 B GLY O 750 188.0 117.3 32.8 21 B TYR N 751 190.2 117.2 32.2 20 B TYR CA 751 190.0 116.2 31.1 19 B TYR CB 751 191.1 116.2 30.1 18 B TYR CG 751 191.2 117.5 29.3 16 B TYR CD1 751 192.4 118.2 29.3 16 B TYR CE1 751 192.6 119.4 28.6 16 B TYR CD2 751 190.1 118.0 28.6 16 B TYR CE2 751 190.2 119.2 27.9 16 B TYR CZ 751 191.4 119.9 27.9 17 B TYR OH 751 191.6 121.1 27.2 18 B TYR C 751 189.7 114.8 31.6 20 B TYR O 751 188.9 114.1 31.1 20 B THR N 752 190.5 114.4 32.6 20 B THR CA 752 190.4 113.1 33.2 20 B THR CB 752 191.5 112.9 34.2 20 B THR OG1 752 192.7 113.1 33.6 21 B THR CG2 752 191.4 111.4 34.7 20 B THR C 752 189.0 113.0 33.9 22 B THR O 752 188.4 111.9 33.9 24 B PHE N 753 188.4 114.0 34.4 22 B PHE CA 753 187.1 114.0 35.0 21 B PHE CB 753 186.7 115.2 35.8 19 B PHE CG 753 185.3 115.2 36.2 18 B PHE CD1 753 184.9 114.4 37.2 17 B PHE CD2 753 184.4 115.9 35.5 18 B PHE CE1 753 183.5 114.3 37.5 18 B PHE CE2 753 183.0 115.8 35.7 19 B PHE CZ 753 182.6 115.0 36.8 19 B PHE C 753 186.1 113.8 33.8 21 B PHE O 753 185.3 112.9 33.8 23 B CYS N 754 186.3 114.6 32.7 22 B CYS CA 754 185.4 114.5 31.5 22 B CYS CB 754 185.8 115.5 30.5 23 B CYS SG 754 185.4 117.2 31.0 23 B CYS C 754 185.5 113.1 30.9 22 B CYS O 754 184.4 112.5 30.6 23 B GLY N 755 186.7 112.5 30.8 22 B GLY CA 755 186.9 111.2 30.2 22 B GLY C 755 186.2 110.2 31.0 24 B GLY O 755 185.3 109.5 30.5 24 B LEU N 756 186.6 110.0 32.3 24 B LEU CA 756 186.0 109.0 33.2 25 B LEU CB 756 186.6 109.0 34.5 25 B LEU CG 756 186.2 107.9 35.5 24 B LEU CD1 756 186.5 106.5 35.0 24 B LEU CD2 756 186.9 108.1 36.8 24 B LEU C 756 184.4 109.2 33.3 26 B LEU O 756 183.7 108.2 33.1 26 B ALA N 757 184.0 110.3 33.7 25 B ALA CA 757 182.5 110.6 33.9 23 B ALA CB 757 182.3 112.0 34.2 22 B ALA C 757 181.7 110.2 32.6 23 B ALA O 757 180.7 109.6 32.8 24 B ALA N 758 182.2 110.5 31.5 23 B ALA CA 758 181.5 110.2 30.2 24 B ALA CB 758 182.2 110.8 29.0 24 B ALA C 758 181.4 108.7 30.0 24 B ALA O 758 180.4 108.2 29.6 24 B LEU N 759 182.5 108.0 30.4 24 B LEU CA 759 182.6 106.5 30.2 24 B LEU CB 759 184.0 106.0 30.5 22 B LEU CG 759 184.9 106.2 29.2 21 B LEU CD1 759 186.2 105.6 29.5 20 B LEU CD2 759 184.2 105.6 28.0 20 B LEU C 759 181.6 105.9 31.2 26 B LEU O 759 180.8 105.0 30.9 26 B VAL N 760 181.6 106.5 32.4 27 B VAL CA 760 180.6 106.0 33.5 26 B VAL CB 760 180.8 106.8 34.7 27 B VAL CG1 760 179.7 106.5 35.7 27 B VAL CG2 760 182.2 106.5 35.4 26 B VAL C 760 179.2 106.2 32.9 27 B VAL O 760 178.4 105.3 33.0 29 B ILE N 761 178.9 107.3 32.3 27 B ILE CA 761 177.6 107.5 31.7 28 B ILE CB 761 177.5 109.0 31.1 28 B ILE CG2 761 176.0 109.2 30.6 27 B ILE CG1 761 177.7 110.0 32.2 27 B ILE CD1 761 177.7 111.4 31.7 27 B ILE C 761 177.4 106.5 30.6 30 B ILE O 761 176.2 106.0 30.4 31 B LEU N 762 178.4 106.2 29.8 32 B LEU CA 762 178.3 105.2 28.7 32 B LEU CB 762 179.4 105.5 27.7 30 B LEU CG 762 179.4 106.8 26.8 29 B LEU CD1 762 180.4 106.7 25.8 28 B LEU CD2 762 178.0 107.0 26.2 27 B LEU C 762 178.4 103.8 29.2 34 B LEU O 762 178.4 102.8 28.5 34 B LYS N 763 178.6 103.7 30.6 36 B LYS CA 763 178.8 102.3 31.2 38 B LYS CB 763 177.5 101.5 31.0 39 B LYS CG 763 176.3 102.1 31.6 42 B LYS CD 763 175.0 101.6 30.9 44 B LYS CE 763 173.8 102.3 31.3 45 B LYS NZ 763 172.7 101.9 30.4 46 B LYS C 763 179.9 101.6 30.5 38 B LYS O 763 179.9 100.4 30.4 39 B LYS N 764 181.0 102.4 30.2 37 B LYS CA 764 182.2 101.8 29.6 37 B LYS CB 764 182.4 102.4 28.2 37 B LYS CG 764 181.3 102.0 27.3 38 B LYS CD 764 181.2 100.6 27.1 39 B LYS CE 764 180.2 100.3 26.0 39 B LYS NZ 764 179.2 101.3 26.0 41 B LYS C 764 183.5 102.0 30.3 38 B LYS O 764 184.5 101.9 29.7 37 B GLU N 765 183.4 102.4 31.6 39 B GLU CA 765 184.7 102.7 32.4 41 B GLU CB 765 184.4 102.8 33.9 42 B GLU CG 765 183.1 103.4 34.3 43 B GLU CD 765 182.0 102.3 34.4 44 B GLU OE1 765 182.0 101.6 35.4 45 B GLU OE2 765 181.2 102.2 33.4 44 B GLU C 765 185.7 101.6 32.2 42 B GLU O 765 186.9 101.9 32.2 43 B ARG N 766 185.3 100.4 32.0 43 B ARG CA 766 186.3 99.3 31.8 45 B ARG CB 766 185.5 97.9 31.6 48 B ARG CG 766 185.1 97.3 33.0 52 B ARG CD 766 183.8 97.8 33.4 55 B ARG NE 766 183.8 98.2 34.8 57 B ARG CZ 766 182.7 98.7 35.5 58 B ARG NH1 766 182.9 99.1 36.8 58 B ARG NH2 766 181.5 98.8 34.9 59 B ARG C 766 187.2 99.5 30.6 44 B ARG O 766 188.2 98.8 30.6 43 B SER N 767 186.8 100.4 29.7 43 B SER CA 767 187.7 100.7 28.6 43 B SER CB 767 186.9 101.6 27.6 43 B SER OG 767 185.8 100.9 27.1 45 B SER C 767 189.0 101.5 28.9 42 B SER O 767 189.8 101.7 28.0 43 B LEU N 768 189.1 101.8 30.2 41 B LEU CA 768 190.4 102.5 30.7 40 B LEU CB 768 190.0 103.7 31.5 39 B LEU CG 768 189.2 104.9 30.8 39 B LEU CD1 768 188.8 105.9 31.9 39 B LEU CD2 768 190.0 105.5 29.7 39 B LEU C 768 191.1 101.6 31.6 39 B LEU O 768 190.5 100.6 32.1 39 B ASN N 769 192.4 101.8 31.8 37 B ASN CA 769 193.2 101.0 32.8 35 B ASN CB 769 194.6 101.1 32.5 35 B ASN CG 769 195.5 100.3 33.5 36 B ASN OD1 769 195.0 100.1 34.6 36 B ASN ND2 769 196.7 100.0 33.1 37 B ASN C 769 192.8 101.7 34.1 35 B ASN O 769 193.5 102.6 34.5 36 B LEU N 770 191.8 101.3 34.8 33 B LEU CA 770 191.4 101.9 36.0 31 B LEU CB 770 190.0 101.3 36.5 29 B LEU CG 770 188.9 101.5 35.5 27 B LEU CD1 770 187.6 101.0 36.1 27 B LEU CD2 770 188.7 103.0 35.1 27 B LEU C 770 192.4 101.8 37.1 32 B LEU O 770 192.4 102.7 38.0 33 B LYS N 771 193.4 101.0 37.0 34 B LYS CA 771 194.4 100.9 38.0 36 B LYS CB 771 195.1 99.6 38.1 39 B LYS CG 771 194.4 98.6 39.0 42 B LYS CD 771 194.0 99.3 40.4 45 B LYS CE 771 193.2 98.4 41.3 46 B LYS NZ 771 191.8 98.0 40.8 47 B LYS C 771 195.5 102.0 37.9 37 B LYS O 771 195.8 102.7 38.9 38 B SER N 772 196.0 102.3 36.7 37 B SER CA 772 196.9 103.3 36.4 37 B SER CB 772 197.5 103.2 35.0 37 B SER OG 772 196.5 103.3 34.0 39 B SER C 772 196.3 104.6 36.6 36 B SER O 772 196.9 105.6 37.0 37 B LEU N 773 195.0 104.7 36.3 36 B LEU CA 773 194.2 105.9 36.5 36 B LEU CB 773 192.9 105.8 35.8 35 B LEU CG 773 191.8 106.8 36.1 35 B LEU CD1 773 192.3 108.3 36.1 34 B LEU CD2 773 190.7 106.7 35.0 35 B LEU C 773 194.1 106.2 38.0 37 B LEU O 773 194.5 107.2 38.5 38 B LEU N 774 193.7 105.1 38.7 36 B LEU CA 774 193.6 105.3 40.2 34 B LEU CB 774 193.2 104.0 40.9 34 B LEU CG 774 193.3 104.1 42.5 34 B LEU CD1 774 192.3 105.1 42.9 33 B LEU CD2 774 193.1 102.8 43.2 34 B LEU C 774 194.9 105.8 40.8 34 B LEU O 774 194.9 106.8 41.5 35 B GLN N 775 196.0 105.2 40.3 34 B GLN CA 775 197.3 105.6 40.8 34 B GLN CB 775 198.3 104.7 40.3 35 B GLN CG 775 199.7 105.0 40.9 39 B GLN CD 775 200.7 103.9 40.6 43 B GLN OE1 775 201.5 103.5 41.5 45 B GLN NE2 775 200.7 103.4 39.3 44 B GLN C 775 197.7 107.1 40.5 33 B GLN O 775 198.2 107.8 41.3 34 B TRP N 776 197.4 107.5 39.2 30 B TRP CA 776 197.7 108.9 38.8 27 B TRP CB 776 197.6 109.0 37.3 25 B TRP CG 776 197.7 110.4 36.8 23 B TRP CD2 776 196.6 111.3 36.6 21 B TRP CE2 776 197.1 112.5 36.1 21 B TRP CE3 776 195.2 111.3 36.8 22 B TRP CD1 776 198.8 111.1 36.4 22 B TRP NE1 776 198.5 112.3 35.9 21 B TRP CZ2 776 196.4 113.6 35.8 22 B TRP CZ3 776 194.4 112.4 36.5 22 B TRP CH2 776 195.0 113.5 36.0 23 B TRP C 776 196.9 109.9 39.6 26 B TRP O 776 197.5 110.8 40.2 26 B VAL N 777 195.6 109.8 39.7 25 B VAL CA 777 194.7 110.8 40.4 24 B VAL CB 777 193.2 110.4 40.3 24 B VAL CG1 777 192.9 109.1 41.0 23 B VAL CG2 777 192.4 111.5 40.8 24 B VAL C 777 195.1 110.9 41.8 26 B VAL O 777 195.2 112.1 42.3 26 B THR N 778 195.4 109.8 42.5 27 B THR CA 778 195.8 109.9 43.9 28 B THR CB 778 195.9 108.5 44.6 27 B THR OG1 778 196.9 107.7 44.0 26 B THR CG2 778 194.5 107.7 44.4 26 B THR C 778 197.1 110.6 44.1 29 B THR O 778 197.4 111.2 45.1 30 B SER N 779 198.0 110.4 43.0 29 B SER CA 779 199.3 111.1 43.1 29 B SER CB 779 200.1 110.6 41.9 30 B SER OG 779 200.4 109.2 42.1 32 B SER C 779 199.1 112.6 42.9 30 B SER O 779 200.1 113.4 43.1 31 B ARG N 780 197.9 113.1 42.5 29 B ARG CA 780 197.7 114.5 42.3 28 B ARG CB 780 196.5 114.7 41.3 28 B ARG CG 780 196.8 114.1 39.9 27 B ARG CD 780 197.7 114.9 39.0 24 B ARG NE 780 199.1 114.9 39.5 23 B ARG CZ 780 199.9 113.8 39.4 22 B ARG NH1 780 199.4 112.6 39.0 22 B ARG NH2 780 201.1 113.9 39.8 21 B ARG C 780 197.4 115.3 43.6 29 B ARG O 780 197.3 116.5 43.5 28 B GLN N 781 197.2 114.7 44.7 30 B GLN CA 781 196.9 115.4 45.9 31 B GLN CB 781 196.2 114.5 47.0 32 B GLN CG 781 195.6 115.4 48.1 32 B GLN CD 781 194.6 114.6 48.9 33 B GLN OE1 781 194.5 113.4 48.9 34 B GLN NE2 781 193.7 115.4 49.6 33 B GLN C 781 198.2 115.9 46.5 52 B GLN O 781 199.2 115.1 46.5 33 B MET N 782 198.3 117.2 4.7 31 B MET CA 782 199.5 117.8 47.2 31 B MET CB 782 199.5 119.3 47.0 30 B MET CG 782 199.3 119.7 45.6 29 B MET SD 782 200.5 118.9 44.5 28 B MET CE 782 201.8 120.1 44.5 28 B MET C 782 199.7 117.4 48.7 33 B MET O 782 198.9 117.8 49.5 33 B ARG N 783 200.8 116.7 48.9 35 B ARG CA 783 201.2 116.3 50.3 36 B ARG CB 783 202.4 115.4 50.3 37 B ARG CG 783 203.6 116.2 49.8 39 B ARG CD 783 204.7 115.4 49.1 41 B ARG NE 783 205.1 114.3 50.0 43 B ARG CZ 783 205.3 113.1 49.6 45 B ARG NH1 783 205.1 112.7 48.4 45 B ARG NH2 783 205.6 112.2 50.6 46 B ARG C 783 201.3 117.4 51.4 36 B ARG O 783 201.2 117.1 52.6 38 B PHE N 784 201.6 118.6 50.9 35 B PHE CA 784 201.7 119.7 51.8 34 B PHE CB 784 202.9 120.6 51.5 34 B PHE CG 784 203.2 121.6 52.5 34 B PHE CD1 784 204.0 121.3 53.6 34 B PHE CD2 784 202.6 122.9 52.4 34 B PHE CE1 784 204.2 122.2 54.6 34 B PHE CE2 784 202.8 123.8 53.4 34 B PHE CZ 784 203.6 123.5 54.5 34 B PHE C 784 200.5 120.6 51.8 33 B PHE O 784 199.9 120.8 52.9 35 B GLU N 785 200.1 121.1 50.7 31 B GLU CA 785 198.9 122.0 50.6 29 B GLU CB 785 198.9 122.7 49.3 30 B GLU CG 785 200.2 123.4 48.9 30 B GLU CD 785 201.2 122.6 48.1 32 B GLU OE1 785 201.1 122.6 46.9 34 B GLU OE2 785 202.0 121.9 48.8 33 B GLU C 785 197.6 121.2 50.8 29 B GLU O 785 196.6 121.8 51.2 28 B GLY N 786 197.7 119.9 50.6 28 B GLY CA 786 196.5 119.0 50.8 27 B GLY C 786 195.5 119.1 49.6 27 B GLY O 786 194.7 118.2 49.5 28 B GLY N 787 195.5 120.2 48.9 26 B GLY CA 787 194.6 120.4 47.8 24 B GLY C 787 195.2 119.6 46.6 23 B GLY O 787 196.3 119.0 46.7 22 B PHE N 788 194.4 119.6 45.5 23 B PHE CA 788 194.9 118.9 44.2 23 B PHE CB 788 193.7 118.1 43.6 22 B PHE CG 788 193.4 116.7 44.2 22 B PHE CD1 788 192.5 116.6 45.2 22 B PHE CD2 788 194.1 115.6 43.8 22 B PHE CE1 788 192.2 115.3 45.8 21 B PHE CE2 788 193.9 114.4 44.4 21 B PHE CZ 788 192.9 114.2 45.4 21 B PHE C 788 195.5 119.7 43.2 22 B PHE O 788 195.2 120.9 43.0 23 B GLN N 789 196.4 119.2 42.4 23 B GLN CA 789 197.1 119.9 41.3 24 B GLN CB 789 198.6 119.6 41.3 23 B GLN CG 789 198.9 118.1 41.0 23 B GLN CD 789 200.4 117.9 41.0 24 B GLN OE1 789 200.9 116.7 40.8 24 B GLN NE2 789 201.2 118.9 41.3 25 B GLN C 789 196.4 119.4 40.0 24 B GLN O 789 195.9 118.2 40.0 25 B GLY N 790 196.5 120.2 39.0 23 B GLY CA 790 195.9 119.8 37.7 20 B GLY C 790 196.6 118.7 36.9 19 B GLY O 790 196.0 117.9 36.3 18 B ARG N 791 198.0 118.8 37.0 18 B ARG CA 791 198.8 117.8 36.2 19 B ARG CB 791 198.9 118.2 34.7 19 B ARG CG 791 198.8 119.8 34.5 19 B ARG CD 791 199.0 120.2 33.0 20 B ARG NE 791 198.9 121.6 32.8 19 B ARG CZ 791 199.6 122.3 31.8 19 B ARG NH1 791 200.3 121.7 30.9 19 B ARG NH2 791 199.5 123.6 31.7 17 B ARG C 791 200.1 117.8 37.0 20 B ARG O 791 200.5 118.7 37.6 20 B CYS N 792 200.8 116.6 36.8 22 B CYS CA 792 202.1 116.4 37.5 23 B CYS CB 792 202.7 115.2 37.0 24 B CYS SG 792 204.1 114.7 37.9 26 B CYS C 792 203.0 117.6 37.4 25 B CYS O 792 203.1 118.2 36.3 26 B ASN N 793 203.7 117.9 38.5 27 B ASN CA 793 204.7 119.0 38.5 27 B ASN CB 793 205.9 118.7 37.6 28 B ASN CG 793 207.0 118.0 38.3 29 B ASN OD1 793 207.1 118.1 39.6 29 B ASN ND2 793 207.9 117.3 37.6 28 B ASN C 793 204.1 120.4 38.2 27 B ASN O 793 204.8 121.4 37.7 27 B LYS N 794 202.8 120.6 38.5 27 B LYS CA 794 202.1 121.8 38.4 26 B LYS CB 794 200.9 121.5 37.5 28 B LYS CG 794 200.7 122.6 36.5 28 B LYS CD 794 201.8 122.6 35.5 27 B LYS CE 794 201.5 123.5 34.4 28 B LYS NZ 794 200.9 124.9 34.8 26 B LYS C 794 201.7 122.2 39.8 26 B LYS O 794 202.0 121.6 40.8 26 B LEU N 795 200.9 123.3 39.9 26 B LEU CA 795 200.5 123.9 41.2 25 B LEU CB 795 200.6 125.4 41.2 24 B LEU CG 795 202.0 126.0 40.8 22 B LEU CD1 795 201.9 127.5 41.1 22 B LEU CD2 795 203.1 125.3 41.5 23 B LEU C 795 199.1 123.5 41.6 25 B LEU O 795 198.3 123.2 40.8 25 B VAL N 796 198.9 123.6 42.9 25 B VAL CA 796 197.5 123.3 43.5 24 B VAL CB 796 197.5 123.5 45.0 25 B VAL CG1 796 197.1 122.3 45.7 26 B VAL CG2 796 198.8 124.1 45.5 26 B VAL C 796 196.6 124.3 43.0 23 B VAL O 796 196.9 125.5 42.7 25 B ASP N 797 195.3 124.0 43.0 23 B ASP CA 797 194.3 125.0 42.6 22 B ASP CB 797 194.3 125.0 41.1 21 B ASP CG 797 193.1 125.9 40.5 21 B ASP OD1 797 192.1 126.1 41.1 22 B ASP OD2 797 193.3 126.4 39.4 22 B ASP C 797 193.0 124.4 43.1 22 B ASP O 797 192.6 123.3 42.9 23 B GLY N 798 192.2 125.2 43.8 23 B GLY CA 798 191.0 124.8 44.4 24 B GLY C 798 189.9 124.2 43.5 25 B GLY O 798 189.2 123.3 44.1 27 B CYS N 799 189.8 124.5 42.3 25 B CYS CA 799 188.7 123.9 41.4 25 B CYS CB 799 188.5 124.5 40.1 26 B CYS SG 799 190.0 124.7 39.0 27 B CYS C 799 189.0 122.4 41.2 26 B CYS O 799 188.1 121.6 41.0 26 B TYR N 800 190.3 122.0 41.3 25 B TYR CA 800 190.7 120.6 41.1 27 B TYR CB 800 192.2 120.5 40.9 26 B TYR CG 800 192.7 121.1 39.6 26 B TYR CD1 800 193.7 122.0 39.6 26 B TYR CE1 800 194.1 122.6 38.4 27 B TYR CD2 800 192.0 120.8 38.4 26 B TYR CE2 800 192.4 121.4 37.2 27 B TYR CZ 800 193.5 122.3 37.2 27 B TYR OH 800 193.9 123.0 36.1 27 B TYR C 800 190.3 119.8 42.3 29 B TYR O 800 190.5 118.6 42.3 30 B SER N 801 189.7 120.4 43.3 30 B SER CA 801 189.2 119.7 44.5 29 B SER CB 801 188.7 120.7 45.5 29 B SER OG 801 189.8 121.7 45.8 28 B SER C 801 188.1 118.9 44.0 30 B SER O 801 187.8 117.8 44.5 31 B PHE N 802 187.4 119.3 42.9 30 B PHE CA 802 186.3 118.6 42.2 29 B PHE CB 802 185.2 119.4 41.8 27 B PHE CG 802 184.1 118.6 41.1 27 B PHE CD1 802 183.1 118.0 41.9 27 B PHE CD2 802 184.1 118.5 39.8 26 B PHE CE1 802 182.1 117.2 41.2 27 B PHE CE2 802 183.2 117.7 39.1 27 B PHE CZ 802 182.2 117.0 39.9 27 B PHE C 802 186.7 117.8 41.0 29 B PHE O 802 186.3 116.6 40.8 32 B TRP N 803 187.4 118.4 40.1 26 B TRP CA 803 187.6 117.7 38.8 22 B TRP CB 803 188.6 118.7 37.9 20 B TRP CG 803 187.8 119.9 37.5 17 B TRP CD2 803 186.6 119.9 36.8 16 B TRP CE2 803 186.3 121.3 36.6 16 B TRP CE3 803 185.7 118.9 36.4 17 B TRP CD1 803 188.2 121.2 37.6 17 B TRP NE1 803 187.3 122.0 37.1 17 B TRP CZ2 803 185.1 121.7 35.9 17 B TRP CZ3 803 184.5 119.3 35.8 17 B TRP CH2 803 184.2 120.7 35.5 17 B TRP C 803 188.7 116.5 39.1 23 B TRP O 803 188.5 115.5 38.5 24 B GLN N 804 189.6 116.6 40.1 24 B GLN CA 804 190.5 115.5 40.5 24 B GLN CB 804 191.8 116.0 41.0 23 B GLN CG 804 192.6 116.8 40.0 24 B GLN CD 804 193.4 115.9 39.1 24 B GLN OE1 804 192.9 114.8 38.7 25 B GLN NE2 804 194.6 116.3 38.7 24 B GLN C 804 189.9 114.6 41.6 26 B GLN O 804 189.7 113.4 41.4 27 B ALA N 805 189.6 115.2 42.8 25 B ALA CA 805 189.0 114.4 43.9 24 B ALA CB 805 188.8 115.3 45.1 23 B ALA C 805 187.7 1.3.8 43.5 24 B ALA O 805 187.3 112.8 44.0 25 B GLY N 806 187.0 114.4 42.5 24 B GLY CA 806 185.7 113.9 42.0 24 B GLY C 806 185.9 112.6 41.4 25 B GLY O 806 185.0 111.8 41.4 26 B LEU N 807 187.1 112.3 40.9 26 B LEU CA 807 187.4 111.0 40.2 28 B LEU CB 807 188.8 111.0 39.6 28 B LEU CG 807 189.0 111.8 38.3 28 B LEU CD1 807 190.5 112.1 38.1 28 B LEU CD2 807 188.5 111.1 37.1 27 B LEU C 807 187.2 109.8 41.1 30 B LEU O 807 186.9 108.7 40.7 31 B LEU N 808 187.5 110.0 42.4 30 B LEU CA 808 187.5 108.9 43.4 30 B LEU CB 808 188.2 109.3 44.6 30 B LEU CG 808 189.7 109.4 44.1 31 B LEU CD1 808 190.4 110.6 44.6 31 B LEU CD2 808 190.5 108.1 44.3 29 B LEU C 808 186.1 108.3 43.6 31 B LEU O 808 185.9 107.1 43.8 32 B PRO N 809 185.0 109.1 43.7 30 B PRO CD 809 185.0 110.6 44.0 30 B PRO CA 809 183.7 108.6 43.8 29 B PRO CB 809 182.8 109.8 43.9 29 B PRO CG 809 183.7 110.7 44.7 30 B PRO C 809 183.4 107.8 42.6 30 B PRO O 809 182.8 106.7 42.6 31 B LEU N 810 183.8 108.3 41.4 30 B LEU CA 810 183.5 107.6 40.1 29 B LEU CB 810 184.0 108.5 39.0 28 B LEU CG 810 183.1 109.7 38.7 27 B LEU CD1 810 183.6 110.5 37.5 27 B LEU CD2 810 181.7 109.3 38.6 27 B LEU C 810 184.3 106.3 40.1 30 B LEU O 810 183.7 105.3 39.6 29 B LEU N 811 185.5 106.3 40.5 32 B LEU CA 811 186.3 105.1 40.5 35 B LEU CB 811 187.8 105.4 40.8 33 B LEU CG 811 188.7 105.8 39.6 32 B LEU CD1 811 189.9 106.5 40.2 31 B LEU CD2 811 189.0 104.6 38.8 30 B LEU C 811 185.8 104.1 41.5 39 B LEU O 811 186.1 102.9 41.4 41 B HIS N 812 185.1 104.5 42.5 43 B HIS CA 812 184.5 103.6 43.5 46 B HIS CB 812 183.9 104.4 44.7 49 B HIS CG 812 184.2 103.7 46.1 51 B HIS CD2 812 183.5 102.8 46.7 51 B HIS ND1 812 185.3 104.0 46.8 52 B HIS CE1 812 185.3 103.3 47.9 51 B HIS NE2 812 184.2 102.5 47.9 51 B HIS C 812 183.5 102.7 42.8 47 B HIS O 812 183.6 101.5 42.9 46 B ARG N 813 182.5 103.4 42.2 48 B ARG CA 813 181.5 102.7 41.5 49 B ARG CB 813 180.7 103.6 40.5 52 B ARG CG 813 179.8 104.6 41.2 56 B ARG CD 813 179.3 105.7 40.2 59 B ARG NE 813 178.2 106.5 40.7 62 B ARG CZ 813 178.2 107.3 41.8 63 B ARG NH1 813 179.3 107.4 42.6 63 B ARG NH2 813 177.0 107.9 42.2 64 B ARG C 813 182.1 101.6 40.6 48 B ARG O 813 181.8 100.5 40.6 49 B ALA N 814 183.0 102.1 39.7 47 B ALA CA 814 183.7 101.2 38.8 46 B ALA CB 814 184.7 102.0 38.0 46 B ALA C 814 184.4 100.0 39.4 46 B ALA O 814 184.1 98.9 39.1 46 B LEU N 815 185.4 100.3 40.3 47 B LEU CA 815 186.1 99.2 41.0 48 B LEU CB 815 187.1 99.8 41.9 47 B LEU CG 815 188.3 100.6 41.4 48 B LEU CD1 815 189.0 101.3 42.4 48 B LEU CD2 815 189.2 99.7 40.6 48 B LEU C 815 185.2 98.3 41.7 49 B LEU O 815 185.2 97.0 41.5 50 B HIS N 816 184.3 98.8 42.4 51 B HIS CA 816 183.3 98.0 43.2 53 B HIS CB 816 182.5 98.9 44.1 55 B HIS CG 816 181.4 98.2 44.7 57 B HIS CD2 816 181.3 97.4 45.8 58 B HIS ND1 816 180.1 98.4 44.3 58 B HIS CE1 816 179.3 97.7 45.0 59 B HIS NE2 816 180.0 97.1 46.0 59 B HIS C 816 182.4 97.3 42.3 54 B HIS O 816 181.8 96.2 42.7 54 B ALA N 817 182.1 97.8 41.1 54 B ALA CA 817 181.2 97.1 40.1 54 B ALA CB 817 180.9 98.0 39.0 54 B ALA C 817 181.9 95.9 39.6 55 B ALA O 817 181.2 95.1 38.9 55 B GLN N 818 183.1 95.7 39.9 56 B GLN CA 818 183.9 94.5 39.5 56 B GLN CB 818 185.2 94.9 38.9 56 B GLN CG 818 184.9 95.7 37.6 57 B GLN CD 818 186.1 96.5 37.2 57 B GLN OE1 818 187.3 96.1 37.3 58 B GLN NE2 818 185.8 97.7 36.7 58 B GLN C 818 184.1 93.8 40.8 57 B GLN O 818 185.0 92.9 40.9 58 B GLY N 819 183.2 94.1 41.8 58 B GLY CA 819 183.3 93.5 43.1 59 B GLY C 819 184.7 93.5 43.7 60 B GLY O 819 185.2 92.5 44.2 61 B ASP N 820 185.3 94.7 43.7 60 B ASP CA 820 186.6 94.8 44.3 59 B ASP CB 820 187.2 96.2 44.0 59 B ASP CG 820 188.8 96.2 44.0 58 B ASP OD1 820 189.3 96.1 42.9 59 B ASP OD2 820 189.4 96.2 45.1 57 B ASP C 820 186.3 94.6 45.8 59 B ASP O 820 185.4 95.2 46.4 59 B PRO N 821 187.1 93.6 46.4 59 B PRO CD 821 187.8 92.6 45.7 59 B PRO CA 821 186.9 93.4 47.8 59 B PRO CB 821 187.5 92.0 48.0 59 B PRO CG 821 188.5 91.9 46.9 59 B PRO C 821 187.6 94.4 48.7 59 B PRO O 821 187.1 94.9 49.7 60 B ALA N 822 188.9 94.8 48.3 57 B ALA CA 822 189.7 95.8 49.1 55 B ALA CB 822 191.1 95.7 48.6 54 B ALA C 822 189.2 97.2 49.2 55 B ALA O 822 189.9 98.0 49.7 55 B LEU N 823 187.9 97.5 48.7 55 B LEU CA 823 187.4 98.8 48.7 55 B LEU CB 823 186.3 99.0 47.7 54 B LEU CG 823 186.7 99.1 46.2 53 B LEU CD1 823 185.5 99.5 45.4 53 B LEU CD2 823 187.8 100.1 46.1 53 B LEU C 823 186.7 99.2 50.1 57 B LEU O 823 185.7 98.6 50.5 57 B SER N 824 187.3 100.3 50.6 58 B SER CA 824 186.8 100.8 51.9 58 B SER CB 824 187.6 102.1 52.3 59 B SER OG 824 187.3 102.5 53.6 59 B SER C 824 185.3 101.0 52.0 59 B SER O 824 184.7 101.3 50.9 59 B MET N 825 184.7 100.9 53.1 60 B MET CA 825 183.3 101.1 53.3 60 B MET CB 825 182.7 100.0 54.0 63 B MET CG 825 182.7 98.6 53.3 66 B MET SD 825 181.8 98.6 51.7 70 B MET CE 825 183.0 97.5 50.6 69 B MET C 825 183.0 102.4 54.0 59 B MET O 825 181.8 102.6 54.4 59 B SER N 826 184.0 103.3 54.1 57 B SER CA 826 183.8 104.6 54.7 55 B SER CB 826 184.3 104.5 56.2 55 B SER OG 826 185.7 104.1 56.2 54 B SER C 826 184.4 105.8 54.1 53 B SER O 826 183.9 106.9 54.2 53 B HIS N 827 185.5 105.6 53.3 52 B HIS CA 827 186.2 106.7 52.7 49 B HIS CB 827 187.5 107.1 53.5 51 B HIS CG 827 187.2 107.4 55.0 52 B HIS CD2 827 187.7 106.8 56.1 52 B HIS ND1 827 186.3 108.3 55.4 52 B HIS CE1 827 186.3 108.4 56.7 53 B HIS NE2 827 187.1 107.5 57.2 53 B HIS C 827 186.7 106.6 51.3 46 B HIS O 827 187.0 105.5 50.8 45 B TRP N 828 186.7 107.8 50.6 42 B TRP CA 828 187.2 107.8 49.2 36 B TRP CB 828 186.9 109.2 48.6 32 B TRP CG 828 185.4 109.5 48.6 29 B TRP CD2 828 184.4 108.7 48.1 27 B TRP CE2 828 183.2 109.4 48.2 26 B TRP CE3 828 184.4 107.4 47.5 26 B TRP CD1 828 184.9 110.7 49.0 28 B TRP NE1 828 183.5 110.6 48.8 27 B TRP CZ2 828 182.0 108.9 47.8 26 B TRP CZ3 828 183.1 106.9 47.1 27 B TRP CH2 828 182.0 107.7 47.3 26 B TRP C 828 188.7 107.7 49.3 36 B TRP O 828 189.3 108.0 50.3 35 B MET N 829 189.3 107.1 48.2 35 B MET CA 829 190.7 106.9 48.3 35 B MET CB 829 191.1 105.8 47.3 35 B MET CG 829 190.3 104.5 47.5 36 B MET SD 829 190.8 103.1 46.5 37 B MET CE 829 192.6 103.3 46.6 35 B MET C 829 191.6 108.1 48.1 35 B MET O 829 192.4 108.2 47.2 35 B PHE N 830 191.4 109.1 49.0 35 B PHE CA 830 192.2 110.3 49.0 34 B PHE CB 830 191.8 111.3 47.9 30 B PHE CG 830 190.5 112.1 48.1 26 B PHE CD1 830 190.6 113.3 48.8 25 B PHE CD2 830 189.3 111.7 47.6 25 B PHE CE1 830 189.4 114.1 48.9 24 B PHE CE2 830 188.2 112.4 47.8 24 B PHE CZ 830 188.2 113.6 48.4 24 B PHE C 830 192.0 111.0 50.4 36 B PHE O 830 190.9 110.7 51.0 37 B HIS N 831 192.9 111.7 50.8 38 B HIS CA 831 192.8 112.4 52.1 38 B HIS CB 831 194.1 113.0 52.5 39 B HIS CG 831 194.4 113.1 54.0 40 B HIS CD2 831 193.7 113.7 55.0 39 B HIS ND1 831 195.5 112.5 54.6 40 B HIS CE1 831 195.4 112.7 55.9 40 B HIS NE2 831 194.4 113.4 56.1 41 B HIS C 831 191.7 113.4 52.1 39 B HIS O 831 191.9 114.6 51.8 40 B GLN N 832 190.5 113.0 52.5 38 B GLN CA 832 189.3 113.9 52.6 39 B GLN CB 832 188.1 113.2 52.9 38 B GLN CG 832 187.8 112.0 52.0 36 B GLN CD 832 186.8 111.1 52.5 35 B GLN OE1 832 185.7 111.5 53.0 36 B GLN NE2 832 187.1 109.8 52.4 34 B GLN C 832 189.5 115.1 53.6 40 B GLN O 832 188.9 116.1 53.5 39 B GLN N 833 190.3 114.8 54.6 42 B GLN CA 833 190.6 115.7 55.7 43 B GLN CB 833 191.3 115.0 56.8 44 B GLN CG 833 191.2 115.7 58.2 45 B GLN CD 833 192.4 115.4 59.1 46 B GLN OE1 833 193.1 114.5 59.0 46 B GLN NE2 833 192.5 116.3 60.1 46 B GLN C 833 191.5 116.9 55.2 42 B GLN O 833 191.1 118.0 55.3 41 B ALA N 834 192.6 116.5 54.6 40 B ALA CA 834 193.5 117.5 54.1 38 B ALA CB 834 194.8 116.9 53.6 37 B ALA C 834 192.9 118.4 53.0 38 B ALA O 834 193.1 119.6 53.0 39 B LEU N 835 192.1 117.7 52.2 38 B LEU CA 835 191.4 118.5 51.1 38 B LEU CB 835 190.7 117.6 50.1 38 B LEU CG 835 189.8 118.3 49.1 38 B LEU CD1 835 190.6 119.3 48.3 38 B LEU CD2 835 189.1 117.4 48.2 38 B LEU C 835 190.4 119.6 51.8 38 B LEU O 835 190.4 120.7 51.3 38 B GLN N 836 189.7 119.1 52.8 38 B GLN CA 836 188.7 120.0 53.4 38 B GLN CB 836 187.9 119.3 54.5 38 B GLN CG 836 186.6 118.7 53.9 38 B GLN CD 836 185.8 117.9 54.9 37 B GLN OE1 836 185.1 118.4 55.8 36 B GLN NE2 836 186.0 116.6 54.8 37 B GLN C 836 189.4 121.2 54.1 37 B GLN O 836 188.9 122.3 54.2 37 B GLU N 837 190.6 121.0 54.6 36 B GLU CA 837 191.4 122.0 55.3 37 B GLU CB 837 192.5 121.4 56.1 36 B GLU CG 837 191.9 120.7 57.4 36 B GLU CD 837 192.9 119.8 58.1 36 B GLU OE1 837 194.1 120.0 58.0 36 B GLU OE2 837 192.5 118.8 58.7 37 B GLU C 837 191.9 123.0 54.3 38 B GLU O 837 191.7 124.2 54.4 39 B TYR N 838 192.5 122.5 53.1 38 B TYR CA 838 193.0 123.4 52.1 35 B TYR CB 838 193.5 122.6 50.9 35 B TYR CG 838 193.9 123.5 49.7 35 B TYR CD1 838 195.1 124.2 49.8 34 B TYR CE1 838 195.4 125.2 48.8 34 B TYR CD2 838 193.1 123.8 48.6 34 B TYR CE2 838 193.4 124.7 47.7 33 B TYR CZ 838 194.6 125.4 47.7 33 B TYR OH 838 194.8 126.4 46.8 33 B TYR C 838 191.8 124.3 51.7 34 B TYR O 838 191.8 125.5 51.8 34 B ILE N 839 190.7 123.6 51.3 32 B ILE CA 839 189.5 124.4 50.9 31 B ILE CB 839 188.3 123.5 50.4 30 B ILE CG2 839 187.3 124.4 49.9 29 B ILE CG1 839 188.7 122.6 49.3 30 B ILE CD1 839 187.5 121.8 48.8 29 B ILE C 839 189.0 125.4 51.9 32 B ILE O 839 188.6 126.5 51.6 35 B LEU N 840 189.0 125.0 53.2 32 B LEU CA 840 188.5 125.9 54.3 32 B LEU CB 840 188.1 125.1 55.5 30 B LEU CG 840 186.7 124.5 55.2 29 B LEU CD1 840 186.5 123.4 56.3 30 B LEU CD2 840 185.6 125.5 55.2 28 B LEU C 840 189.5 127.0 54.6 32 B LEU O 840 189.1 128.2 54.7 32 B MET N 841 190.7 126.6 54.9 32 B MET CA 841 191.8 127.5 55.3 33 B MET CB 841 192.9 126.8 55.9 33 B MET CG 841 192.6 126.0 57.2 34 B MET SD 841 193.9 125.8 58.3 35 B MET CE 841 194.3 124.1 58.0 34 B MET C 841 192.3 128.4 54.2 34 B MET O 841 192.3 129.6 54.3 35 B CYS N 842 192.7 127.8 53.1 35 B CYS CA 842 193.3 128.5 52.0 34 B CYS CB 842 194.4 127.7 51.4 34 B CYS SG 842 195.6 127.2 52.6 36 B CYS C 842 192.4 129.1 50.8 34 B CYS O 842 192.8 130.1 50.2 35 B CYS N 843 191.3 128.5 50.5 34 B CYS CA 843 190.5 128.9 49.4 34 B CYS CB 843 190.2 127.8 48.4 32 B CYS SG 843 191.7 126.8 48.1 31 B CYS C 843 189.3 129.7 49.6 36 B CYS O 843 188.4 129.9 48.7 37 B GLN N 844 189.1 130.3 50.8 38 B GLN CA 844 187.9 131.1 51.1 39 B GLN CB 844 187.4 130.6 52.4 39 B GLN CG 844 186.0 130.8 52.6 39 B GLN CD 844 185.4 129.8 53.6 40 B GLN OE1 844 184.2 129.6 53.6 40 B GLN NE2 844 186.3 129.2 54.4 39 B GLN C 844 188.2 132.6 51.1 40 B GLN O 844 189.2 133.0 51.6 40 B CYS N 845 187.3 133.4 50.5 41 B CYS CA 845 187.5 134.8 50.5 43 B CYS CB 845 187.1 135.4 49.1 43 B CYS SG 845 186.9 137.2 49.0 44 B CYS C 845 186.6 135.4 51.5 45 B CYS O 845 185.4 135.1 51.6 46 B PRO N 846 187.1 136.2 52.4 45 B PRO CD 846 188.5 136.7 52.5 45 B PRO CA 846 186.4 136.9 53.5 45 B PRO CB 846 187.4 137.9 54.0 45 B PRO CG 846 188.7 137.3 53.9 45 B PRO C 846 185.1 137.5 53.0 44 B PRO O 846 184.0 137.2 53.6 46 B ALA N 847 185.2 138.3 52.0 42 B ALA CA 847 184.1 139.0 51.3 41 B ALA CB 847 184.6 140.0 50.4 41 B ALA C 847 183.1 138.1 50.7 40 B ALA O 847 182.0 138.6 50.2 40 B GLY N 848 183.4 136.8 50.5 39 B GLY CA 848 182.4 135.9 49.9 38 B GLY C 848 183.2 135.3 48.7 37 B GLY O 848 184.1 135.9 48.2 38 B GLY N 849 182.8 134.2 48.2 35 B GLY CA 849 183.5 133.5 47.1 32 B GLY C 849 184.7 132.7 47.6 30 B GLY O 849 185.3 133.0 48.6 29 B LEU N 850 184.9 131.6 46.8 29 B LEU CA B50 186.1 130.8 47.1 28 B LEU CB 850 185.7 129.3 47.1 28 B LEU CG 850 185.0 128.5 48.2 28 B LEU CD1 850 185.9 128.2 49.4 26 B LEU CD2 850 183.7 129.3 48.6 26 B LEU C 850 187.1 131.1 46.0 28 B LEU O 850 186.7 131.8 45.0 27 B LEU N 851 188.2 130.5 46.0 27 B LEU CA 851 189.2 130.8 45.0 28 B LEU CB 851 189.8 132.2 45.3 28 B LEU CG 851 190.3 132.4 46.8 28 B LEU CD1 851 191.7 131.8 47.0 28 B LEU CD2 851 190.2 133.8 47.2 27 B LEU C 851 190.3 129.8 44.7 30 B LEU O 851 190.3 128.7 45.3 31 B ASP N 852 191.1 130.1 43.7 29 B ASP CA 852 192.2 129.2 43.3 29 B ASP CB 852 193.0 129.9 42.2 29 B ASP CG 852 194.2 129.1 41.7 30 B ASP OD1 852 194.6 128.1 42.3 31 B ASP OD2 852 194.8 129.5 40.7 32 B ASP C 852 193.0 128.8 44.5 29 B ASP O 852 192.9 127.6 44.9 28 B LYS N 853 193.9 129.7 44.9 28 B LYS CA 853 194.8 129.4 46.0 27 B LYS CB 853 196.1 128.9 45.5 24 B LYS CG 853 196.9 129.9 44.6 23 B LYS CD 853 198.3 129.5 44.3 22 B LYS CE 853 198.3 128.1 43.7 22 B LYS NZ 853 197.5 128.0 42.4 22 B LYS C 853 194.9 130.8 46.5 29 B LYS O 853 194.5 131.8 45.9 27 B PRO N 854 195.6 131.0 47.7 32 B PRO CD 854 196.1 129.9 48.6 32 B PRO CA 854 195.8 132.3 48.3 33 B PRO CB 854 196.4 132.0 49.6 33 B PRO CG 854 197.1 130.7 49.4 32 B PRO C 854 196.6 133.2 47.4 34 B PRO O 854 197.6 132.9 46.8 35 B GLY N 855 196.0 134.4 47.2 35 B GLY CA 855 196.7 135.4 46.3 36 B GLY C 855 195.8 135.6 45.1 37 B GLY O 855 195.8 136.7 44.6 39 B LYS N 856 195.1 134.6 44.7 36 B LYS CA 856 194.2 134.6 43.6 34 B LYS CB 856 193.9 133.2 43.1 34 B LYS CG 856 195.1 132.5 42.7 33 B LYS CD 856 195.9 133.3 41.7 34 B LYS CE 856 197.2 132.7 41.3 35 B LYS NZ 856 197.1 131.8 40.2 36 B LYS C 856 192.9 135.3 44.0 35 B LYS O 856 192.6 135.6 45.1 36 B SER N 857 192.1 135.8 42.9 35 B SER CA 857 190.8 136.4 43.1 34 B SER CB 857 190.6 137.5 42.0 34 B SER OG 857 191.4 138.6 42.2 37 B SER C 857 189.7 135.4 43.1 34 B SER O 857 189.8 134.4 42.5 34 B ARG N 858 188.6 135.8 43.7 32 B ARG CA 858 187.4 135.0 43.8 31 B ARG CB 858 186.5 135.5 44.9 30 B ARG CG 858 186.0 136.9 44.7 30 B ARG CD 858 185.4 137.5 46.0 30 B ARG NE 858 184.5 138.6 45.7 30 B ARG CZ 858 183.6 139.1 46.5 30 B ARG NH1 858 183.4 138.4 47.6 31 B ARG NH2 858 182.8 140.0 46.1 30 B ARG C 858 186.6 135.1 42.5 30 B ARG O 858 186.8 136.0 41.7 30 B ASP N 859 185.8 134.0 42.2 29 B ASP CA 859 185.0 134.0 41.0 28 B ASP CB 859 185.8 133.9 39.7 29 B ASP CG 859 186.6 132.7 39.6 29 B ASP OD1 859 186.1 131.6 39.5 30 B ASP OD2 859 187.9 132.8 39.7 30 B ASP C 859 184.0 132.9 41.2 28 B ASP O 859 184.2 132.0 42.1 28 B PHE N 860 182.9 132.9 40.4 28 B PHE CA 860 181.9 131.9 40.5 28 B PHE CB 860 180.7 132.3 39.7 28 B PHE CG 860 180.3 133.7 40.1 28 B PHE CD1 860 180.6 134.8 39.4 28 B PHE CD2 860 179.6 133.9 41.3 28 B PHE CE1 860 180.3 136.1 39.8 27 B PHE CE2 860 179.3 135.2 41.8 27 B PHE CZ 860 179.6 136.3 41.0 27 B PHE C 860 182.3 130.5 40.1 29 B PHE O 860 181.8 129.5 40.6 31 B TYR N 861 183.3 130.4 39.2 28 B TYR CA 861 183.9 129.1 38.7 25 B TYR CB 861 184.9 129.3 37.6 22 B TYR CG 861 185.7 128.1 37.3 19 B TYR CD1 861 185.1 126.9 36.9 17 B TYR CE1 861 185.9 125.7 36.7 15 B TYR CD2 861 187.1 128.1 37.5 16 B TYR CE2 861 187.9 127.0 37.3 15 B TYR CZ 861 187.2 125.8 36.9 15 B TYR OH 861 188.0 124.7 36.8 14 B TYR C 861 184.5 128.3 39.9 26 B TYR O 861 184.2 127.2 40.2 26 B HIS N 862 185.4 129.0 40.6 27 B HIS CA 862 186.1 128.4 41.8 27 B HIS CB 862 187.3 129.2 42.2 25 B HIS CG 862 188.3 129.2 41.2 25 B HIS CD2 862 189.4 128.4 41.0 25 B HIS ND1 862 188.4 130.2 40.2 26 B HIS CE1 862 189.4 130.0 39.4 27 B HIS NE2 862 190.1 128.9 39.9 25 B HIS C 862 185.1 128.3 43.0 28 B HIS O 862 185.3 127.4 43.9 29 B THR N 863 184.1 129.2 43.1 28 B THR CA 863 183.2 129.2 44.1 30 B THR CB 863 182.2 130.3 44.0 30 B THR OG1 863 182.9 131.6 44.2 32 B THR CG2 863 181.0 130.2 45.1 29 B THR C 863 182.4 127.8 44.0 30 B THR O 863 182.4 127.0 44.9 30 B CYS N 864 182.0 127.6 42.8 30 B CYS CA 864 181.3 126.4 42.4 29 B CYS CB 864 180.7 126.4 41.0 29 B CYS SG 864 180.2 124.8 40.4 30 B CYS C 864 182.1 125.1 42.6 29 B CYS O 864 181.7 124.2 43.2 29 B TYR N 865 183.3 125.2 42.1 28 B TYR CA 865 184.1 124.0 42.2 28 B TYR CB 865 185.1 123.8 41.0 28 B TYR CG 865 184.3 123.5 39.8 26 B TYR CD1 865 183.8 124.5 38.9 26 B TYR CE1 865 182.9 124.2 37.9 26 B TYR CD2 865 183.9 122.2 39.5 26 B TYR CE2 865 183.0 121.9 38.4 25 B TYR CZ 865 182.5 122.9 37.6 26 B TYR OH 865 181.7 122.6 36.6 26 B TYR C 865 184.7 123.7 43.6 29 B TYR O 865 184.9 122.5 44.0 30 B CYS N 866 185.1 124.7 44.3 30 B CYS CA 866 185.6 124.5 45.7 30 B CYS CB 866 186.1 125.9 46.3 30 B CYS SG 866 187.6 126.5 45.6 31 B CYS C 866 184.5 123.9 46.6 30 B CYS O 866 184.8 122.9 47.3 31 B LEU N 867 183.3 124.5 46.5 29 B LEU CA 867 182.2 124.0 47.3 29 B LEU CB 867 181.0 124.9 47.2 27 B LEU CG 867 181.3 126.3 47.8 26 B LEU CD1 867 180.0 127.1 47.6 26 B LEU CD2 867 181.7 126.1 49.2 25 B LEU C 867 181.9 122.6 46.8 30 B LEU O 867 181.7 121.7 47.6 31 B SER N 868 181.9 122.3 45.5 31 B SER CA 868 181.6 121.0 44.9 30 B SER CB 868 181.7 121.1 43.4 29 B SER OG 868 180.5 121.7 42.8 28 B SER C 868 182.5 120.0 45.5 30 B SER O 868 182.1 118.9 46.0 31 B GLY N 869 183.8 120.3 45.4 31 B GLY CA 869 184.9 119.4 45.9 32 B GLY C 869 184.8 119.2 47.4 34 B GLY O 869 185.4 118.2 47.9 35 B LEU N 870 184.2 120.1 48.2 35 B LEU CA 870 184.2 120.0 49.6 34 B LEU CB 870 183.7 121.3 50.2 33 B LEU CG 870 183.7 121.6 51.8 31 B LEU CD1 870 185.1 121.4 52.3 30 B LEU CD2 870 183.2 122.9 52.1 29 B LEU C 870 183.1 118.9 49.9 35 B LEU O 870 183.3 118.0 50.7 35 B SER N 871 181.9 119.1 49.3 35 B SER CA 871 180.8 118.2 49.4 35 B SER CB 871 179.7 118.6 48.4 36 B SER OG 871 178.6 117.8 48.6 36 B SER C 871 181.2 116.8 49.1 36 B SER O 871 180.8 115.9 49.9 37 B ILE N 872 182.0 116.6 48.1 36 B ILE CA 872 182.5 115.3 47.8 37 B ILE CB 872 183.2 115.2 46.3 35 B ILE CG2 872 184.0 114.0 46.1 33 B ILE CG1 872 182.1 115.3 45.3 35 B ILE CD1 872 182.6 115.3 43.9 35 B ILE C 872 183.4 114.7 48.9 37 B ILE O 872 183.2 113.6 49.3 38 B ALA N 873 184.4 115.5 49.3 38 B ALA CA 873 185.3 115.1 50.4 39 B ALA CB 873 186.5 116.1 50.5 39 B ALA C 873 184.7 114.8 51.7 39 B ALA O 873 185.3 114.2 52.6 38 B GLN N 874 183.5 115.4 52.0 39 B GLN CA 874 182.9 115.2 53.2 40 B GLN CB 874 182.4 116.5 53.8 38 B GLN CG 874 181.3 117.2 53.1 36 B GLN CD 874 181.0 118.6 53.7 36 B GLN OE1 874 179.9 119.1 53.4 36 B GLN NE2 874 181.9 119.1 54.5 34 B GLN C 874 181.7 114.2 53.2 42 B GLN O 874 181.2 113.8 54.2 42 B HIS N 875 181.4 113.8 52.0 44 B HIS CA 875 180.3 112.9 51.8 46 B HIS CB 875 179.1 113.5 51.0 45 B HIS CG 875 178.4 114.6 51.7 45 B HIS CD2 875 177.7 115.6 51.2 45 B HIS ND1 875 178.4 114.7 53.0 45 B HIS CE1 875 177.7 115.8 53.4 45 B HIS NE2 875 177.2 116.3 52.3 45 B HIS C 875 180.7 111.5 51.1 48 B HIS O 875 181.0 111.5 49.9 48 B PHE N 876 180.7 110.5 51.9 51 B PHE CA 876 181.0 109.2 51.4 53 B PHE CB 876 182.0 108.4 52.2 51 B PHE CG 876 182.2 107.0 51.8 51 B PHE CD1 876 183.2 106.7 50.8 51 B PHE CD2 876 181.4 106.0 52.2 51 B PHE CE1 876 183.4 105.4 50.3 51 B PHE CE2 876 181.5 104.7 51.7 50 B PHE CZ 876 182.5 104.4 50.8 51 B PHE C 876 179.7 108.3 51.3 56 B PHE O 876 178.8 108.5 52.2 56 B GLY N 877 179.7 107.4 50.4 58 B GLY CA 877 178.5 106.5 50.2 62 B GLY C 877 178.9 105.3 49.3 64 B GLY O 877 179.6 105.5 48.3 64 B SER N 878 178.5 104.1 49.7 66 B SER CA 878 178.9 102.9 48.9 67 B SER CB 878 180.2 102.4 49.4 67 B SER OG 878 180.8 101.5 48.4 67 B SER C 878 177.7 101.9 49.1 69 B SER O 878 177.9 100.9 49.8 69 B GLY N 879 176.6 102.2 48.5 70 B GLY CA 879 175.4 101.3 48.6 71 B GLY C 879 174.7 101.7 49.8 72 B GLY O 879 174.1 102.8 49.9 72 B ALA N 880 174.7 100.8 50.8 72 B ALA CA 880 174.1 101.0 52.1 72 B ALA CB 880 173.8 99.7 52.8 72 B ALA C 880 174.9 102.0 52.9 72 B ALA O 880 174.4 102.6 53.9 73 B MET N 881 176.2 102.0 52.6 72 B MET CA 881 177.2 102.9 53.3 71 B MET CB 881 178.6 102.5 53.0 72 B MET CG 881 179.1 101.2 53.6 74 B MET SD 881 178.0 99.9 53.2 75 B MET CE 881 177.4 99.5 54.9 75 B MET C 881 177.0 104.3 53.1 69 B MET O 881 176.7 104.7 52.0 69 B LEU N 882 177.3 105.1 54.1 68 B LEU CA 882 177.2 106.6 54.1 66 B LEU CB 882 175.7 107.0 54.3 66 B LEU CG 882 174.8 107.2 53.1 67 B LEU CD1 882 175.5 107.8 51.9 67 B LEU CD2 882 174.1 105.8 52.7 67 B LEU C 882 178.0 107.1 55.3 64 B LEU O 882 177.6 107.0 56.4 65 B HIS N 883 179.2 107.6 55.0 62 B HIS CA 883 180.0 108.2 56.0 60 B HIS CB 883 181.3 107.3 56.3 60 B HIS CG 883 182.2 107.8 57.4 60 B HIS CD2 883 182.8 109.0 57.6 60 B HIS ND1 883 182.6 107.0 58.4 61 B HIS CE1 883 183.4 107.7 59.2 60 B HIS NE2 883 183.5 108.9 58.8 60 B HIS C 883 180.5 109.6 55.7 58 B HIS O 883 181.0 109.9 54.6 58 B ASP N 884 180.1 110.5 56.5 56 B ASP CA 884 180.5 111.9 56.3 53 B ASP CB 884 179.3 112.8 56.7 52 B ASP CG 884 178.1 112.6 55.7 52 B ASP OD1 884 177.2 113.5 55.7 51 B ASP OD2 884 178.1 111.6 55.0 52 B ASP C 884 181.7 112.3 57.2 52 B ASP O 884 181.9 111.6 58.2 52 B VAL N 885 182.4 113.2 56.8 51 B VAL CA 885 183.6 113.7 57.5 48 B VAL CB 885 184.9 113.2 56.9 47 B VAL CG1 885 186.1 113.9 57.6 46 B VAL CG2 885 185.1 111.7 57.2 46 B VAL C 885 183.5 115.2 57.3 48 B VAL O 885 183.9 115.7 56.3 50 B VAL N 886 182.9 116.0 58.3 47 B VAL CA 886 182.8 117.4 58.2 48 B VAL CB 886 181.5 117.9 58.6 48 B VAL CG1 886 181.4 119.4 58.3 47 B VAL CG2 886 180.4 117.2 57.8 48 B VAL C 886 183.9 118.0 59.1 49 B VAL O 886 183.9 117.7 60.2 50 B MET N 887 184.8 118.8 58.5 50 B MET CA 887 185.8 119.5 59.2 49 B MET CB 887 187.0 119.8 58.4 49 B MET CG 887 187.7 118.5 57.9 49 B MET SD 887 188.1 117.5 59.3 49 B MET CE 887 189.6 118.2 59.8 48 B MET C 887 185.3 120.8 59.8 50 B MET O 887 184.5 121.5 59.1 50 B GLY N 888 185.8 121.2 60.9 52 B GLY CA 888 185.4 122.5 61.5 53 B GLY C 888 184.0 122.5 62.1 54 B GLY O 888 183.4 121.5 62.4 54 B VAL N 889 183.4 123.7 62.2 55 B VAL CA 889 182.0 123.8 62.7 56 B VAL CB 889 181.6 125.3 62.7 56 B VAL CG1 889 180.7 125.6 61.5 56 B VAL CG2 889 181.0 125.7 64.0 57 B VAL C 889 181.1 122.9 61.9 57 B VAL O 889 181.2 122.9 60.7 59 B PRO N 890 180.3 122.1 62.5 57 B PRO CD 890 180.0 122.0 64.0 58 B PRO CA 890 179.4 121.2 61.8 57 B PRO CB 890 178.7 120.4 62.9 58 B PRO CG 890 178.6 121.4 64.0 58 B PRO C 890 178.4 121.9 60.8 57 B PRO O 890 177.6 121.2 60.1 57 B GLU N 891 178.3 123.2 60.9 56 B GLU CA 891 177.4 124.0 60.0 56 B GLU CB 891 177.3 125.4 60.6 58 B GLU CG 891 176.3 125.5 61.8 60 B GLU CD 891 176.8 124.8 63.0 62 B GLU OE1 891 178.1 124.7 63.2 62 B GLU OE2 891 176.0 124.3 63.8 63 B GLU C 891 178.1 124.0 58.7 56 B GLU O 891 177.6 124.5 57.7 56 B ASN N 892 179.3 123.4 58.6 53 B ASN CA 892 180.1 123.4 57.4 51 B ASN CB 892 181.6 123.2 57.7 49 B ASN CG 892 182.2 124.5 58.4 47 B ASN OD1 892 183.3 124.4 58.9 46 B ASN ND2 892 181.5 125.6 58.4 45 B ASN C 892 179.7 122.2 56.5 50 B ASN O 892 180.4 121.9 55.5 52 B VAL N 893 178.6 121.6 56.7 49 B VAL CA 893 178.2 120.5 55.9 47 B VAL CB 893 177.6 119.3 56.6 47 B VAL CG1 893 176.4 119.7 57.4 48 B VAL CG2 893 177.3 118.2 55.7 48 B VAL C 893 177.3 121.0 54.8 46 B VAL O 893 176.2 121.6 55.1 46 B LEU N 894 177.7 120.7 53.5 45 B LEU CA 894 176.9 121.1 52.3 44 B LEU CB 894 177.9 121.5 51.2 43 B LEU CG 894 179.0 122.5 51.6 42 B LEU CD1 894 180.2 122.4 50.6 41 B LEU CD2 894 178.4 123.8 51.6 42 B LEU C 894 176.0 120.0 51.8 43 B LEU O 894 176.3 118.8 52.1 44 B GLN N 895 175.0 120.4 51.0 42 B GLN CA 895 174.2 119.4 50.4 42 B GLN CB 895 173.1 120.1 49.5 43 B GLN CG 895 172.1 120.7 50.4 45 B GLN CD 895 171.3 119.7 51.2 46 B GLN OE1 895 170.5 119.0 50.7 46 B GLN NE2 895 171.7 119.7 52.5 46 B GLN C 895 175.1 118.5 49.5 42 B GLN O 895 176.1 119.0 49.0 42 B PRO N 896 174.7 117.2 49.3 41 B PRO CD 896 173.5 116.5 49.8 40 B PRO CA 896 175.5 116.3 48.5 40 B PRO CB 896 174.9 115.0 48.9 39 B PRO CG 896 173.5 115.3 49.1 40 B PRO C 896 175.3 116.6 46.9 39 B PRO O 896 174.3 117.1 46.5 39 B THR N 897 176.4 116.3 46.2 38 B THR CA 897 176.5 116.5 44.8 36 B THR CB 897 177.6 117.6 44.4 36 B THR OG1 897 177.5 117.9 43.0 37 B THR CG2 897 179.0 117.1 44.7 35 B THR C 897 176.7 115.2 44.1 34 B THR O 897 177.4 114.3 44.6 35 B HIS N 898 176.1 115.0 42.9 33 B HIS CA 898 176.2 113.7 42.2 33 B HIS CB 898 175.1 113.7 41.1 32 B HIS CG 898 175.0 112.4 40.4 32 B HIS CD2 898 173.9 111.6 40.0 32 B HIS ND1 898 176.1 111.6 40.0 32 B HIS CE1 898 175.7 110.5 39.3 31 B HIS NE2 898 174.4 110.5 39.4 32 B HIS C 898 177.6 113.8 41.5 32 B HIS O 898 177.8 114.7 40.7 33 B PRO N 899 178.5 112.9 41.7 32 B PRO CD 899 178.4 111.8 42.6 32 B PRO CA 899 179.9 112.9 41.1 32 B PRO CB 899 180.6 111.8 41.9 32 B PRO CG 899 179.6 110.9 42.2 33 B PRO C 899 180.0 112.8 39.6 31 B PRO O 899 181.2 112.9 39.1 32 B VAL N 900 179.0 112.5 38.9 30 B VAL CA 900 179.1 112.4 37.4 29 B VAL CB 900 178.2 111.2 36.9 28 B VAL CG1 900 178.2 111.2 35.4 26 B VAL CG2 900 178.7 109.9 37.4 27 B VAL C 900 178.6 113.7 36.8 30 B VAL O 900 179.4 114.3 36.0 30 B TYR N 901 177.4 114.2 37.2 29 B TYR CA 901 176.8 115.4 36.7 29 B TYR CB 901 175.3 115.2 36.7 28 B TYR CG 901 174.8 114.1 35.8 28 B TYR CD1 901 174.4 112.9 36.3 29 B TYR CE1 901 174.0 1118 35.5 29 B TYR CD2 901 174.8 114.3 34.4 28 B TYR CE2 901 174.5 113.2 33.6 29 B TYR CZ 901 174.1 112.0 34.1 29 B TYR OH 901 173.7 111.0 33.3 28 B TYR C 901 177.1 116.7 37.5 30 B TYR O 901 176.9 117.8 37.0 30 B ASN N 902 177.5 116.5 38.8 30 B ASN CA 902 177.8 117.6 39.7 30 B ASN CB 902 179.0 118.5 39.2 30 B ASN CG 902 179.6 119.3 40.4 29 B ASN OD1 902 179.6 118.8 41.5 29 B ASN ND2 902 180.1 120.4 40.1 29 B ASN C 902 176.6 118.5 39.9 29 B ASN O 902 176.6 119.7 39.7 29 B ILE N 903 175.5 117.9 40.3 30 B ILE CA 903 174.3 118.6 40.7 31 B ILE CB 903 173.3 118.8 39.5 30 B ILE CG2 903 174.0 119.5 38.4 30 B ILE CG1 903 172.7 117.5 39.0 30 B ILE CD1 903 171.6 117.6 38.0 28 B ILE C 903 173.6 117.7 41.7 33 B ILE O 903 174.1 116.5 41.8 34 B GLY N 904 172.7 118.2 42.4 35 B GLY CA 904 172.0 117.4 43.4 36 B GLY C 904 171.6 116.0 42.9 37 B GLY O 904 171.0 115.9 41.9 37 B PRO N 905 171.9 115.0 43.7 38 B PRO CD 905 172.7 115.1 44.9 38 B PRO CA 905 171.6 113.6 43.4 39 B PRO CB 905 172.0 112.9 44.7 38 B PRO CG 905 173.2 113.7 45.2 38 B PRO C 905 170.2 113.4 43.1 40 B PRO O 905 169.8 112.6 42.3 41 B ASP N 906 169.4 114.2 43.8 42 B ASP CA 906 167.9 114.2 43.6 45 B ASP CB 906 167.3 114.9 44.8 47 B ASP CG 906 168.0 116.2 45.2 50 B ASP OD1 906 169.0 116.2 45.9 51 B ASP OD2 906 167.5 117.3 44.8 51 B ASP C 906 167.4 114.8 42.4 44 B ASP O 906 166.4 114.5 41.8 45 B LYS N 907 168.2 115.8 41.9 44 B LYS CA 907 168.0 116.5 40.6 43 B LYS CB 907 168.9 117.7 40.5 43 B LYS CG 907 168.7 11e.7 41.6 42 B LYS CD 907 167.3 119.2 41.5 42 B LYS CE 907 167.0 120.0 42.7 43 B LYS NZ 907 165.6 120.6 42.6 44 B LYS C 907 168.2 115.5 39.5 43 B LYS O 907 167.5 115.5 38.5 43 B VAL N 908 169.3 114.8 39.6 42 B VAL CA 908 169.7 113.8 38.6 42 B VAL CB 908 171.0 113.0 39.1 41 B VAL CG1 908 171.2 111.9 38.1 41 B VAL CG2 908 172.1 114.0 39.1 40 B VAL C 908 168.5 112.8 38.5 42 B VAL O 908 168.0 112.5 37.5 42 B ILE N 909 168.0 112.3 39.7 42 B ILE CA 909 166.9 111.4 39.7 42 B ILE CB 909 166.7 110.9 41.1 42 B ILE CG2 909 165.4 110.0 41.1 42 B ILE CG1 909 167.9 110.2 41.6 42 B ILE CD1 909 167.9 109.8 43.1 42 B ILE C 909 165.7 112.1 39.2 43 B ILE O 909 165.0 111.6 38.2 43 B GLN N 910 165.3 113.2 39.7 43 B GLN CA 910 164.2 114.0 39.3 44 B GLN CB 910 164.1 115.3 40.0 45 B GLN CG 910 162.8 116.0 40.0 47 B GLN CD 910 162.8 117.4 40.7 48 B GLN OE1 910 161.8 118.1 40.6 49 B GLN NE2 910 163.9 117.7 41.5 49 B GLN C 910 164.1 114.2 37.7 44 B GLN O 910 163.1 113.9 37.1 44 B ALA N 911 165.2 114.7 37.2 44 B ALA CA 911 165.2 115.0 35.7 43 B ALA CB 911 166.4 115.8 35.4 44 B ALA C 911 165.2 113.8 34.8 43 B ALA O 911 164.5 113.8 33.9 42 B THR N 912 165.9 112.7 35.2 43 B THR CA 912 166.0 111.5 34.4 43 B THR CB 912 167.0 110.5 34.9 43 B THR OG1 912 166.8 110.3 36.3 45 B THR CG2 912 168.5 111.1 34.7 43 B THR C 912 164.7 110.8 34.3 43 B THR O 912 164.3 110.4 33.1 45 B THR N 913 163.9 110.7 35.4 43 B THR CA 913 162.6 110.0 35.3 42 B THR CB 913 162.2 109.5 36.7 42 B THR OG1 913 161.3 110.4 37.3 43 B THR CG2 913 163.4 109.3 37.6 42 B THR C 913 161.6 110.9 34.6 41 B THR O 913 160.6 110.4 34.0 42 B HIS N 914 161.7 112.2 34.7 40 B HIS CA 914 160.7 113.0 34.1 39 B HIS CB 914 160.8 114.5 34.5 38 B HIS CG 914 160.1 115.4 33.5 37 B HIS CD2 914 158.8 115.9 33.5 37 B HIS ND1 914 160.7 115.9 32.4 37 B HIS CE1 914 159.8 116.6 31.7 36 B HIS NE2 914 158.7 116.6 32.3 37 B HIS C 914 160.9 113.0 32.5 40 B HIS O 914 160.0 112.9 31.8 40 B PHE N 915 162.2 113.1 32.1 40 B PHE CA 915 162.5 113.0 30.7 40 B PHE CB 915 164.0 113.5 30.4 39 B PHE CG 915 164.1 115.0 30.5 37 B PHE CD1 915 164.8 115.6 31.6 37 B PHE CD2 915 163.5 115.8 29.6 37 B PHE CE1 915 164.9 117.0 31.7 36 B PHE CE2 915 163.6 117.2 29.7 36 B PHE CZ 915 164.3 117.8 30.7 36 B PHE C 915 162.2 111.6 30.1 41 B PHE O 915 162.0 111.4 28.9 41 B LEU N 916 162.2 110.7 31.0 42 B LEU CA 916 162.0 109.3 30.7 44 B LEU CB 916 162.3 108.4 31.9 43 B LEU CG 916 163.4 107.3 31.8 43 B LEU CD1 916 164.4 107.7 30.7 44 B LEU CD2 916 164.1 107.2 33.1 43 B LEU C 916 160.5 109.1 30.3 45 B LEU O 916 160.2 108.3 29.5 44 B GLN N 917 159.6 110.0 30.7 47 B GLN CA 917 158.2 110.0 30.4 48 B GLN CB 917 157.5 111.1 31.1 50 B GLN CG 917 157.6 111.1 32.6 51 B GLN CD 917 157.1 112.4 33.2 53 B GLN OE1 917 157.8 113.0 34.1 54 B GLN NE2 917 156.0 113.0 32.7 53 B GLN C 917 158.1 110.3 28.9 49 B GLN O 917 157.0 110.1 28.3 50 B LYS N 918 159.2 110.8 28.3 51 B LYS CA 918 159.2 111.1 26.9 52 B LYS CB 918 159.7 112.5 26.6 54 B LYS CG 918 159.0 113.6 27.3 55 B LYS CD 918 159.5 113.7 28.8 56 B LYS CE 918 158.5 114.5 29.6 57 B LYS NZ 918 158.2 115.9 29.1 58 B LYS C 918 160.0 110.1 26.1 53 B LYS O 918 160.8 109.4 26.7 54 B PRO N 919 159.7 109.9 24.8 55 B PRO CD 919 158.6 110.5 24.0 55 B PRO CA 919 160.5 108.9 24.1 55 B PRO CB 919 159.5 108.5 23.0 55 B PRO CG 919 158.8 109.8 22.7 55 B PRO C 919 161.7 109.6 23.5 56 B PRO O 919 161.7 110.8 23.2 57 B VAL N 920 162.7 108.8 23.3 58 B VAL CA 920 164.0 109.2 22.7 59 B VAL CB 920 164.9 108.0 22.5 58 B VAL CG1 920 166.1 108.5 21.6 58 B VAL CG2 920 165.4 107.5 23.8 57 B VAL C 920 163.6 109.7 21.3 62 B VAL O 920 162.9 109.0 20.6 62 B PRO N 921 163.9 111.0 20.9 65 B PRO CD 921 164.6 112.0 21.7 65 B PRO CA 921 163.5 111.5 19.6 68 8 PRO CB 921 164.3 112.8 19.5 67 B PRO CG 921 164.3 113.3 20.9 66 B PRO C 921 163.7 110.5 18.5 71 B PRO O 921 164.8 110.5 17.9 71 B GLY N 922 162.7 109.7 18.3 76 B GLY CA 922 162.8 108.6 17.3 81 B GLY C 922 162.7 109.0 15.8 85 B GLY O 922 162.6 110.2 15.5 86 B PHE N 923 162.9 108.1 14.9 88 B PHE CA 923 162.8 108.3 13.5 91 B PHE CB 923 164.3 108.2 12.9 92 B PHE CG 923 165.3 108.7 13.9 94 B PHE CD1 923 165.8 110.0 13.8 94 B PHE CD2 923 165.9 107.8 14.9 94 B PHE CE1 923 166.7 110.5 14.8 94 B PHE CE2 923 166.8 108.3 15.8 94 B PHE CZ 923 167.2 109.6 15.7 94 B PHE C 923 162.0 107.2 12.9 92 B PHE O11 923 162.5 106.1 12.7 92 B PHE O12 923 160.7 107.4 12.8 92 B ZIN ZN 1000 191.3 126.5 39.1 29 Z FPP P 2001 196.5 125.9 33.1 25 F FPP O 2001 196.4 127.5 33.0 26 F FPP O1 2001 197.9 125.5 32.5 26 F FPP O2 2001 196.3 125.5 34.6 27 F FPP O3 2001 195.3 125.3 32.2 26 F FPP C 2001 195.4 124.0 31.7 25 F FPP C1 2001 193.1 123.5 30.5 23 F FPP C2 2001 193.9 123.4 31.5 25 F FPP C3 2001 191.7 123.0 30.5 23 F FPP C4 2001 193.6 124.1 29.1 24 F FPP C5 2001 191.4 122.1 31.7 22 F FPP C6 2001 188.9 121.7 32.5 18 F FPP C7 2001 189.9 121.5 31.7 20 F FPP C8 2001 188.9 122.8 33.6 17 F FPP C9 2001 187.7 120.9 32.4 17 F FPP C10 2001 186.4 121.6 31.9 16 F FPP C11 2001 185.2 120.7 31.9 15 F FPP C12 2001 184.0 121.0 31.4 16 F FPP C13 2001 183.8 122.3 30.6 15 F FPP C14 2001 182.8 120.0 31.5 16 F FPP P1 2001 197.0 124.2 35.2 27 F FPP O4 2001 196.2 123.9 36.6 27 F FPP O5 2001 196.8 123.0 34.2 28 F FPP O6 2001 198.5 124.5 35.5 27 F SCH C 2002 188.1 132.3 33.6 32 I SCH C1 2002 187.5 129.8 33.0 32 I SCH C2 2002 186.4 129.9 34.0 32 I SCH C3 2002 186.9 130.8 35.2 33 I SCH N 2002 187.2 132.1 34.7 33 I SCH C4 2002 187.9 131.2 32.5 32 I SCH CL1 2002 183.7 124.3 33.8 31 I SCH C5 2002 190.2 127.3 30.3 32 I SCH C6 2002 184.7 125.6 33.2 33 I SCH C7 2002 186.0 125.7 33.5 33 I SCH C8 2002 188.2 126.9 33.5 33 I SCH C9 2002 189.1 126.5 32.4 34 I SCH C10 2002 184.8 127.7 32.0 39 I SCH C11 2002 190.3 128.2 29.2 32 I SCH C12 2002 189.4 129.2 29.0 31 I SCH N1 2002 188.3 129.3 29.8 30 I SCH C13 2002 187.0 128.9 31.8 33 I SCH C14 2002 184.1 126.6 32.5 36 I SCH BR1 2002 191.8 128.0 28.0 32 I SCH BR2 2002 184.0 129.0 31.0 54 I SCH C15 2002 188.2 128.5 30.9 32 I SCH C16 2002 186.2 127.7 32.3 36 I SCH C17 2002 189.2 127.5 31.2 33 I SCH C18 2002 186.8 126.7 33.1 33 I SCH C19 2002 186.3 137.0 35.1 32 I SCH C20 2002 186.2 138.2 36.0 32 I SCH C21 2002 186.5 135.7 35.8 32 I SCH C22 2002 187.5 135.8 37.1 32 I SCH N2 2002 187.4 138.3 36.9 32 I SCH C23 2002 187.3 137.1 37.8 32 I SCH C24 2002 187.0 134.6 34.9 33 I SCH O 2002 185.9 133.1 36.4 35 I SCH C25 2002 186.7 133.2 35.4 33 I HOH OH2 1002 187.9 129.7 16.9 16 W HOH OH2 1003 201.5 124.1 44.5 15 W HOH OH2 1004 203.3 117.4 25.9 18 W HOH OH2 1005 198.0 115.2 20.3 16 W HOH OH2 1007 199.8 114.9 34.8 16 W HOH OH2 1009 191.9 123.0 17.7 21 W HOH OH2 1011 196.8 117.6 19.2 8 W HOH OH2 1012 204.8 119.9 34.9 16 W HOH OH2 1016 202.7 109.1 23.5 34 W HOH OH2 1019 194.1 118.5 18.8 24 W HOH OH2 1020 179.4 133.1 21.3 26 W HOH OH2 1021 203.2 120.1 32.8 14 W HOH OH2 1022 206.9 126.2 33.3 26 W HOH OH2 1023 204.5 127.0 36.5 27 W HOH OH2 1024 181.2 104.2 22.9 33 W HOH OH2 1026 177.7 137.8 20.1 25 W HOH OH2 1032 205.1 124.6 37.1 18 W HOH OH2 1033 197.7 103.4 28.1 34 W HOH OH2 1034 203.3 119.7 48.3 29 W HOH OH2 1038 190.3 120.7 16.9 27 W HOH OH2 1039 209.4 125.2 32.9 21 W HOH OH2 1042 192.4 121.3 45.2 23 W HOH OH2 1044 193.8 139.7 8.4 21 W HOH OH2 1045 191.5 118.1 18.3 27 W HOH OH2 1046 201.7 115.0 46.8 43 W HOH OH2 1050 179.8 127.6 15.8 32 W HOH OH2 1051 189.8 139.0 25.5 31 W HOH OH2 1052 206.2 133.4 14.1 33 W HOH OH2 1054 191.0 115.7 17.4 41 W HOH OH2 1055 193.7 139.2 5.6 17 W HOH OH2 1061 175.6 137.8 26.3 29 W HOH OH2 1063 202.3 139.1 14.3 36 W HOH OH2 1064 195.2 113.3 18.7 37 W HOH OH2 1065 207.2 124.5 11.5 22 W HOH OH2 1066 178.6 139.0 43.6 38 W HOH OH2 1067 185.2 129.7 16.4 35 W HOH OH2 1068 185.9 125.9 10.0 33 W HOH OH2 1070 185.2 114.3 22.0 34 W HOH OH2 1071 206.4 108.4 11.4 46 W HOH OH2 1073 201.6 111.0 25.1 23 W HOH OH2 1074 200.2 107.5 25.7 36 W HOH OH2 1075 211.4 126.6 32.0 20 W HOH OH2 1076 207.2 134.3 16.9 47 W HOH OH2 1077 203.8 112.5 35.2 18 W HOH OH2 1078 207.5 128.7 32.0 24 W HOH OH2 1080 187.0 111.5 12.5 43 W HOH OH2 1081 203.3 111.3 11.6 21 W HOH OH2 1082 177.7 125.8 16.7 43 W HOH OH2 1084 174.6 122.2 14.4 34 W HOH OH2 1085 203.1 127.6 9.2 23 W HOH OH2 1087 207.9 136.9 21.9 37 W HOH OH2 1089 211.4 129.9 29.4 33 W HOH OH2 1090 179.0 102.9 34.6 41 W HOH OH2 1091 184.6 127.9 11.0 31 W HOH OH2 1092 211.9 125.9 29.6 29 W HOH OH2 1093 201.2 109.8 38.8 42 W HOH OH2 1095 198.4 109.2 24.6 35 W HOH OH2 1096 187.2 123.9 11.8 39 W HOH OH2 1097 190.1 102.7 22.4 41 W HOH OH2 1098 184.9 158.2 8.1 31 W HOH OH2 1099 186.6 127.7 18.2 28 W HOH OH2 1100 186.7 124.8 7.7 39 W HOH OH2 1102 200.8 137.2 27.8 44 W HOH OH2 1103 191.8 141.4 18.1 42 W HOH OH2 1104 213.1 113.6 16.5 32 W HOH OH2 1105 203.6 117.6 41.3 15 W HOH OH2 1106 187.5 106.2 46.3 45 W HOH OH2 1107 178.8 115.1 47.8 27 W HOH OH2 1109 188.6 100.8 24.0 46 W HOH OH2 1110 204.0 130.4 42.5 30 W HOH OH2 1111 211.2 123.0 30.0 29 W HOH OH2 1112 176.2 127.7 13.0 36 W HOH OH2 1113 199.9 106.7 44.2 24 W HOH OH2 1114 186.2 98.5 22.2 38 W HOH OH2 1115 198.1 142.0 12.9 65 W HOH OH2 1116 174.3 118.5 31.6 31 W HOH OH2 1117 220.4 119.4 25.1 37 W HOH OH2 1118 208.7 132.2 48.7 42 W HOH OH2 1119 174.7 107.7 35.8 45 W HOH OH2 1120 182.3 99.5 23.2 47 W HOH OH2 1121 200.4 132.2 32.8 63 W HOH OH2 1122 197.1 114.6 14.9 50 W HOH OH2 1123 210.7 127.4 27.8 32 W HOH OH2 1124 162.3 133.7 25.6 39 W HOH OH2 1125 213.2 127.7 22.0 39 W HOH OH2 1126 219.8 125.6 31.4 54 W HOH OH2 1127 198.4 103.0 31.4 37 W HOH OH2 1128 209.9 135.1 24.0 44 W HOH OH2 1129 200.6 107.7 21.9 55 W HOH OH2 1130 172.2 143.3 28.2 33 W HOH OH2 1131 195.0 111.4 47.5 33 W HOH OH2 1132 201.6 109.1 13.1 63 W HOH OH2 1133 214.3 129.8 29.5 46 W HOH OH2 1134 211.5 124.2 17.5 44 W HOH OH2 1135 188.7 114.2 16.3 45 W HOH OH2 1136 168.0 122.5 22.2 35 W HOH OH2 1137 177.2 140.7 24.4 28 W HOH OH2 1138 218.6 124.5 26.1 44 W HOH OH2 1139 194.7 141.2 4.4 35 W HOH OH2 1140 210.8 119.7 16.2 25 W HOH OH2 1141 181.0 138.9 23.8 31 W HOH OH2 1142 177.2 111.6 46.8 63 W HOH OH2 1143 185.4 151.4 10.4 33 W HOH OH2 1144 172.2 138.7 17.7 52 W HOH OH2 1145 214.5 101.9 15.6 45 W HOH OH2 1146 213.8 106.7 19.5 38 W HOH OH2 1147 218.0 123.3 49.2 43 W HOH OH2 1148 200.3 96.8 26.4 53 W HOH OH2 1149 210.7 133.1 17.2 48 W HOH OH2 1150 202.9 135.0 10.9 33 W HOH OH2 1151 177.8 140.9 41.6 27 W HOH OH2 1152 220.4 124.4 40.8 58 W HOH OH2 1155 195.5 123.4 17.9 36 W HOH OH2 1156 174.3 101.1 16.3 50 W HOH OH2 1157 202.9 135.0 7.6 48 W HOH OH2 1158 189.3 106.7 17.8 31 W HOH OH2 1159 176.7 143.5 24.6 35 W HOH OH2 1160 196.1 123.7 20.6 31 W HOH OH2 1161 205.0 103.4 15.4 59 W HOH OH2 1162 171.6 121.4 14.4 35 W HOH OH2 1163 193.6 143.4 17.5 46 W HOH OH2 1164 193.7 140.7 1.6 35 W HOH OH2 1165 213.9 127.4 33.1 31 W HOH OH2 1166 210.2 128.9 31.6 20 W HOH OH2 1167 178.5 120.3 11.6 54 W HOH OH2 1168 204.5 122.0 41.6 33 W HOH OH2 1169 169.5 142.2 37.6 40 W HOH OH2 1170 205.0 117.8 45.9 57 W HOH OH2 1171 201.9 120.8 2.8 60 W HOH OH2 1172 216.1 115.2 17.4 32 W HOH OH2 1173 208.4 116.8 41.5 29 W HOH OH2 1174 218.5 125.0 46.5 63 W HOH OH2 1175 156.5 125.2 36.4 43 W HOH OH2 1176 206.0 130.7 32.9 36 W HOH OH2 1177 206.0 118.8 48.3 43 W HOH OH2 1178 204.0 132.3 13.1 34 W HOH OH2 1179 190.8 100.7 25.6 54 W HOH OH2 1181 172.0 129.8 16.6 32 W HOH OH2 1182 159.5 126.2 29.6 52 W HOH OH2 1183 Z07.7 122.3 7.1 36 W HOH OH2 1184 215.1 121.3 17.6 44 W HOH OH2 1185 203.5 127.3 33.5 51 W HOH OH2 1186 192.0 143.7 6.4 40 W HOH OH2 1187 206.3 136.8 17.2 48 W HOH OH2 1188 211.7 90.0 38.0 36 W HOH OH2 1189 201.0 105.6 19.2 53 W HOH OH2 1190 204.8 136.9 12.4 47 W HOH OH2 1191 176.9 133.5 8.2 34 W HOH OH2 1193 187.0 140.9 31.4 40 W HOH OH2 1194 205.6 123.8 40.0 28 W HOH OH2 1195 204.8 103.1 26.5 49 W HOH OH2 1196 176.0 151.6 22.3 51 W HOH OH2 1197 187.7 114.0 13.1 37 W HOH OH2 1198 204.4 138.5 24.0 34 W HOH OH2 1200 194.0 117.9 9.4 56 W HOH OH2 1201 159.6 117.8 26.7 60 W HOH OH2 1202 185.7 122.3 13.2 33 W HOH OH2 1203 180.7 147.4 35.9 33 W HOH OH2 1204 188.9 120.0 14.5 48 W HOH OH2 1205 173.4 107.8 39.8 71 W HOH OH2 1206 216.1 122.6 19.8 44 W HOH OH2 1207 206.3 120.0 41.8 46 W HOH OH2 1208 213.1 117.8 43.5 42 W HOH OH2 1209 210.8 127.1 23.2 40 W HOH OH2 1210 193.1 116.5 16.3 36 W HOH OH2 1211 190.3 123.2 65.5 48 W HOH OH2 1212 177.9 141.9 45.3 49 W HOH OH2 1213 182.1 99.6 32.0 49 W HOH OH2 1214 211.4 120.5 11.4 56 W HOH OH2 1215 208.8 126.6 12.3 30 W HOH OH2 1216 211.1 129.9 18.4 38 W HOH OH2 1217 165.0 105.0 26.9 58 W HOH OH2 1219 190.4 122.2 6.3 55 W HOH OH2 1220 209.9 116.7 47.6 49 W HOH OH2 1221 196.4 107.6 18.8 70 W HOH OH2 1222 183.3 158.3 20.2 33 W HOH OH2 1223 215.2 128.1 24.6 53 W HOH OH2 1224 174.6 146.0 5.0 50 W HOH OH2 1225 200.4 105.0 36.7 35 W HOH OH2 1226 191.0 142.2 10.9 50 W HOH OH2 1227 157.0 122.0 39.3 57 W HOH OH2 1228 210.3 130.6 38.8 51 W HOH OH2 1229 209.5 122.9 10.2 46 W HOH OH2 1230 196.1 118.8 7.2 48 W HOH OH2 1231 174.7 140.7 30.0 29 W HOH OH2 1232 189.5 159.0 14.9 40 W HOH OH2 1233 171.5 117.6 46.7 30 W HOH OH2 1234 162.2 118.9 27.6 44 W HOH OH2 1235 207.6 98.1 25.6 37 W HOH OH2 1236 201.1 100.8 44.0 35 W HOH OH2 1237 208.5 131.3 35.9 47 W HOH OH2 1238 185.4 148.8 10.4 32 W HOH OH2 1239 211.7 125.4 12.9 48 W HOH OH2 1240 212.7 108.8 18.1 42 W HOH OH2 1241 217.1 120.5 34.6 58 W HOH OH2 1242 211.9 94.9 26.9 55 W HOH OH2 1243 192.2 146.3 23.6 55 W HOH OH2 1244 189.4 144.7 26.3 60 W HOH OH2 1245 168.5 107.9 26.2 37 W HOH OH2 1246 170.2 147.1 12.0 49 W HOH OH2 1247 194.8 108.7 48.0 36 W HOH OH2 1248 210.9 118.6 13.9 33 W HOH OH2 1249 201.1 114.6 53.7 38 W HOH OH2 1250 186.8 149.3 5.7 46 W HOH OH2 1251 216.5 128.1 31.1 56 W HOH OH2 1252 179.2 126.9 57.9 31 W HOH OH2 1253 202.5 102.9 28.7 42 W HOH OH2 1254 213.1 122.9 13.3 44 W HOH OH2 1255 195.9 115.9 17.0 53 W HOH OH2 1256 196.3 142.9 17.1 53 W HOH OH2 1257 213.3 126.6 19.3 50 W HOH OH2 125B 175.9 138.8 21.7 57 W HOH OH2 1259 182.6 158.5 23.3 55 W HOH OH2 1260 211.8 118.5 53.4 51 W HOH OH2 1261 203.6 138.7 6.0 63 W HOH OH2 1263 200.2 141.6 8.4 51 W HOH OH2 1264 202.7 134.4 25.6 46 W HOH OH2 1265 218.7 123.2 36.6 52 W HOH OH2 1266 203.5 132.1 32.8 48 W HOH OH2 1267 211.3 109.7 12.3 60 W HOH OH2 1268 191.3 113.0 18.2 53 W HOH OH2 1269 183.8 98.2 27.8 57 W HOH OH2 1270 168.9 121.4 47.5 62 W HOH OH2 1271 209.9 125.3 8.5 61 W HOH OH2 1272 180.3 140.3 48.3 55 W HOH OH2 1273 199.5 109.3 19.4 47 W HOH OH2 1274 199.3 107.3 58.9 65 W HOH OH2 1275 205.0 118.6 5.8 41 W HOH OH2 1276 206.1 115.3 5.2 57 W HOH OH2 1277 171.1 131.4 20.4 46 W HOH OH2 1278 160.7 127.3 37.1 51 W HOH OH2 1279 211.8 102.7 53.5 62 W HOH OH2 1281 221.0 113.1 44.8 80 W HOH OH2 1282 190.0 140.1 30.7 83 W HOH OH2 1283 172.1 148.3 25.2 57 W HOH OH2 1284 176.9 110.4 53.0 39 W HOH OH2 1285 203.1 115.6 43.0 51 W HOH OH2 1286 168.7 105.2 25.9 52 W HOH OH2 1287 192.1 123.8 2.2 46 W HOH OH2 1288 173.6 145.4 24.6 44 W HOH OH2 1289 196.7 111.5 26.0 29 W HOH OH2 1290 166.0 117.8 38.C 30 W HOH OH2 1291 180.8 140.9 39.6 36 W HOH OH2 1292 212.1 128.0 25.6 51 W HOH OH2 1293 190.8 133.8 1.7 35 W HOH OH2 1295 189.7 110.1 53.4 63 W HOH OH2 1296 178.9 131.5 58.4 63 W HOH OH2 1297 203.7 96.2 34.8 69 W HOH OH2 1298 210.8 120.2 56.4 71 W HOH OH2 1299 205.6 129.3 3.4 68 W HOH OH2 1300 193.9 142.0 9.6 55 W HOH OH2 1301 194.9 112.9 60.3 46 W HOH OH2 1302 180.0 112.3 47.5 48 W HOH OH2 1303 208.7 113.9 47.9 65 W HOH OH2 1304 164.7 126.1 19.9 54 W HOH OH2 1305 219.4 118.6 21.8 53 W HOH OH2 1306 178.8 132.9 10.4 48 W HOH OH2 1307 202.2 108.5 36.5 37 W HOH OH2 1308 161.6 127.4 42.1 69 W HOH OH2 1309 203.4 106.7 34.9 29 W HOH OH2 1310 198.1 118.7 53.9 39 W HOH OH2 1311 216.9 104.4 16.0 71 W HOH OH2 1312 160.1 112.5 21.4 52 W HOH OH2 1313 219.1 104.3 19.5 55 W HOH OH2 1314 213.2 110.9 15.8 46 W HOH OH2 1315 186.7 133.3 55.5 43 W HOH OH2 1316 200.6 104.9 26.6 68 W HOH OH2 1317 206.1 105.8 39.1 47 W HOH OH2 1318 191.0 111.8 55.0 45 W HOH OH2 1319 190.5 131.0 53.0 62 W HOH OH2 1320 187.9 150.2 14.9 50 W HOH OH2 1321 180.9 107.7 14.6 51 W HOH OH2 1322 194.7 147.1 18.0 81 W HOH OH2 1323 198.3 99.2 54.4 51 W HOH OH2 1324 188.5 151.6 27.6 62 W HOH OH2 1325 163.5 120.3 41.0 54 W HOH OH2 1326 205.8 131.2 36.0 50 W HOH OH2 1327 183.3 147.4 37.3 72 W HOH OH2 1328 203.0 139.0 17.0 62 W HOH OH2 1329 186.9 149.0 12.6 57 W HOH OH2 1330 189.4 122.2 11.7 60 W HOH OH2 1331 206.7 105.9 41.8 51 W HOH OH2 1332 199.4 98.5 31.9 73 W HOH OH2 1333 201.2 140.6 20.4 41 W HOH OH2 1334 186.7 124.1 5.1 71 W HOH OH2 1335 184.3 137.8 41.1 35 W HOH OH2 1336 189.3 157.5 22.7 37 W HOH OH2 1337 185.9 147.2 27.7 55 W HOH OH2 1338 202.4 140.2 23.6 65 W HOH OH2 1339 169.8 139.3 22.0 55 W HOH OH2 1340 159.0 121.2 41.4 58 W HOH OH2 1341 186.8 105.5 18.7 48 W HOH OH2 1342 173.7 127.7 14.0 59 W HOH OH2 1343 172.9 134.6 9.0 52 W HOH OH2 1344 183.7 120.7 56.4 26 W HOH OH2 1345 189.8 147.5 14.3 28 W HOH OH2 1346 193.7 121.1 4.5 60 W HOH OH2 1347 176.9 130.9 9.6 53 W HOH OH2 1348 173.5 117.7 54.3 55 W HOH OH2 1349 201.4 131.2 43.4 68 W HOH OH2 1350 175.1 137.5 18.7 44 W HOH OH2 1351 179.6 138.3 50.6 42 W HOH OH2 1352 194.7 114.4 13.2 74 W HOH OH2 1353 197.7 103.3 58.0 48 W HOH OH2 1354 186.7 143.6 30.9 50 W HOH OH2 1355 174.0 123.5 53.0 43 W HOH OH2 1356 183.6 148.1 3.5 61 W HOH OH2 1357 170.1 144.3 27.5 39 W HOH OH2 1358 166.6 142.0 19.9 61 W HOH OH2 1359 161.6 125.4 23.7 60 W HOH OH2 1360 175.1 135.3 10.2 49 W HOH OH2 1361 192.9 115.8 62.8 78 W HOH OH2 1362 176.9 109.0 14.8 82 W HOH OH2 1363 202.2 130.1 6.7 55 W HOH OH2 1364 196.1 106.8 22.2 59 W HOH OH2 1365 156.5 125.4 30.5 72 W HOH OH2 1366 203.2 96.4 38.6 69 W HOH OH2 1367 193.3 130.3 57.4 56 W HOH OH2 1368 180.2 149.2 33.9 71 W HOH OH2 1369 218.9 125.7 34.7 59 W HOH OH2 1370 187.1 144.0 27.9 55 W HOH OH2 1371 183.3 150.7 20.8 51 W HOH OH2 1372 176.0 148.4 29.7 56 W HOH OH2 1373 191.4 141.9 0.8 54 W HOH OH2 1374 213.7 125.2 44.1 40 W HOH OH2 1375 176.4 104.1 21.0 48 W HOH OH2 1376 216.4 112.2 14.3 52 W HOH OH2 1377 197.5 152.8 17.5 64 W HOH OH2 1378 184.1 144.9 0.9 50 W HOH OH2 1379 208.9 .20.2 41.9 54 W HOH OH2 1380 183.8 109.8 54.8 32 W HOH OH2 1381 214.4 113.8 37.6 46 W HOH OH2 1382 212.4 121.8 16.5 45 W HOH OH2 1383 187.9 142.5 0.9 66 W HOH OH2 1384 206.5 100.5 21.0 63 W HOH OH2 1385 158.0 131.5 31.9 65 W HOH OH2 1386 173.8 146.6 28.2 60 W HOH OH2 1388 172.8 135.5 54.3 56 W HOH OH2 1389 217.8 116.5 28.5 71 W HOH OH2 1390 216.5 97.0 26.3 55 W HOH OH2 1391 175.2 124.9 15.1 69 W HOH OH2 1392 206.3 117.0 43.7 82 W HOH OH2 1393 168.1 124.1 46.2 73 W HOH OH2 1394 179.1 134.0 56.6 56 W HOH OH2 1395 169.2 108.0 29.3 60 W HOH OH2 1396 173.5 143.2 3.9 55 W HOH OH2 1397 159.1 118.5 39.3 67 W HOH OH2 1398 189.5 124.2 7.7 39 W HOH OH2 1399 211.8 92.2 39.5 48 W HOH OH2 1400 196.5 142.5 6.1 86 W HOH OH2 1401 212.6 126.9 16.6 59 W HOH OH2 1402 165.5 130.5 21.0 69 W HOH OH2 1403 203.0 132.7 27.6 50 W HOH OH2 1404 177.1 102.9 26.1 65 W HOH OH2 1405 174.6 105.9 21.8 47 W HOH OH2 1406 212.5 130.4 21.4 72 W HOH OH2 1407 214.2 128.8 27.0 81 W HOH OH2 1408 183.5 141.5 39.6 65 W HOH OH2 1409 163.4 128.6 24.0 38 W HOH OH2 1410 216.1 118.5 49.3 67 W HOH OH2 1411 210.6 118.0 42.4 47 W HOH OH2 1412 177.9 147.7 37.4 57 W HOH OH2 1413 185.0 135.9 56.1 52 W HOH OH2 1414 218.0 90.3 39.9 70 W HOH OH2 1415 207.6 131.2 13.5 42 W HOH OH2 1416 203.9 130.1 38.9 68 W HOH OH2 1417 165.4 136.5 32.1 43 W HOH OH2 1418 187.6 140.8 28.3 50 W HOH OH2 1419 206.7 133.7 32.6 77 W HOH OH2 1420 186.6 146.2 31.1 63 W HOH OH2 1421 189.5 104.6 19.5 76 W HOH OH2 1422 208.6 111.3 9.7 70 W HOH OH2 1423 202.3 133.4 59.6 77 W HOH OH2 1424 215.2 126.8 35.8 66 W HOH OH2 1425 217.6 116.9 15.3 47 W HOH OH2 1426 159.9 118.2 29.6 51 W HOH OH2 1427 174.2 132.9 7.3 41 W HOH OH2 1428 180.6 101.6 22.1 61 W HOH OH2 1429 171.0 109.3 35.2 72 W HOH OH2 1430 197.1 110.9 58.2 64 W HOH OH2 1431 183.4 105.8 11.6 57 W HOH OH2 1432 195.0 153.0 15.4 65 W HOH OH2 1433 201.5 137.6 3.0 53 W HOH OH2 1434 195.4 147.5 21.1 81 W HOH OH2 1435 203.9 111.2 54.4 71 W HOH OH2 1436 215.8 107.4 17.8 70 W HOH OH2 1437 174.5 145.8 31.0 66 W HOH OH2 1438 181.7 156.1 25.3 77 W HOH OH2 3001 183.5 132.9 37.3 27 W HOH OH2 3002 186.6 131.2 28.9 12 W HOH OH2 3003 190.7 132.1 42.0 16 W HOH OH2 3004 189.8 134.7 39.6 48 W HOH OH2 3005 189.5 138.1 45.9 50 W HOH OH2 3006 191.9 125.9 35.9 35 W HOH OH2 3007 187.7 136.6 27.0 30 W HOH OH2 3008 197.9 122.3 38.1 25 W HOH OH2 3009 196.1 126.3 38.5 31 W HOH OH2 3010 200.5 130.8 28.8 26 W HOH OH2 3011 197.9 126.1 29.9 16 W HOH OH2 3012 195.3 127.3 29.3 19 W HOH OH2 3013 193.7 128.1 31.9 37 W HOH OH2 3014 200.4 126.4 31.4 39 W HOH OH2 3015 183.4 134.8 27.0 30 W HOH OH2 3016 187.2 134.1 29.8 34 W

EXAMPLE 6 Phasing, Model Building and Refinement

The structure of the crystal form described in Examples 1-3 was solved by molecular replacement, as implemented in XPLOR [Yale University, ©1992, distributed by Molecular Simulations, Inc.; see, e.g., Blundell & Johnson, supra; Meth. Enzymol., vol. 114 and 115, H. W. Wyckoff et al., eds., Academic Press (1985)], using a 2.2 Å resolution model of unliganded FPT as the search model (Beese et al., 1997, Science 275:1800-1804). The structure of the FPT:FPP:SCH66381 complex was highly refined and used as the starting point for further structure determinations. After rigid body refinement using XPLOR, the refinement of each additional structure started from a model of FPT retaining the bound FPP, but with the inhibitor and its associated waters removed. The inhibitors or peptides were built using INSIGHT and QUANTA and fit into the initial omit electron density with CHAIN [J. Sack, J. Molecular Graphics 6:224-225]. The structure was refined by several cycles of model building and positional refinement using XPLOR. Positions of discrete water molecules were taken from positive (Fo-Fc),α_(calc) difference density peaks if a hydrogen bonding pattern to protein, peptide, inhibitors or solvent atoms could be established.

EXAMPLE 7 Structure Determination of FPT:αHFP: CVIM Co-crystals

Co-crystals of FPT:αHFP:CVIM were grown as described in Example 2. Data on these crystals was collected as described in Example 5 and the structure determined as described in Example 6. The structure clearly showed the position of αHFP and the CVIM peptide. Refinement statistics are shown in Table 1 and the coordinates are shown in Table 2.

EXAMPLE 8 Structure Determination of FPT:FPP:SCH66381 Co-crystals

Co-crystals of FPT:FPP:SCH66381 were grown as described in Example 3. Data on these crystals was collected as described in Example 5 and the structure determined as described in Example 6. The structure clearly showed the positions of FPP and SCH66381. Refinement statistics are shown in Table 1 and the coordinates are shown in Table 3.

EXAMPLE 9 Structure Determination of FPT:FPP:SCH66701 Co-crystals

Co-crystals of FPT:FPP:SCH66701 were grown as described in Example 3. Data on these crystals was collected as described in Example 5 and the structure determined as described in Example 6. The structure clearly showed the positions of FPP and SCH66701. Refinement statistics are shown in Table 1 and the coordinates are shown in Table 4.

EXAMPLE 10 Structure Determination of FPT:FPP:SCH69132 Co-crystals

Co-crystals of FPT:FPP:SCH69132 were grown as described in Example 3. Data on these crystals was collected as described in Example 5 and the structure determined as described in Example 6. The structure clearly showed the positions of FPP and SCH69132. Refinement statistics are shown in Table 1 and the coordinates are shown in Table 5.

6 1 4 PRT Artificial Sequence Description of Artificial Sequence Peptide 1 Cys Val Ile Xaa 1 2 4 PRT Artificial Sequence Description of Artificial Sequence Peptide 2 Cys Val Leu Ser 1 3 4 PRT Artificial Sequence MOD_RES (1) ACETYLATION 3 Cys Val Phe Met 1 4 4 PRT Artificial Sequence Description of Artificial Sequence Ca1a2X Peptide 4 Cys Xaa Xaa Xaa 5 1134 DNA Rattus norvegicus 5 atggcggcca ctgagggggt cggggaatct gcgccaggcg gtgagccggg acagccagag 60 cagccgccgc ccccgcctcc tccgccgcca gcacagcagc cgcaggaaga agagatggcg 120 gccgaggccg gggaagcagc ggcgtcccct atggacgacg ggtttctgag cctggactcg 180 cccacctatg tcttgtacag ggacagggca gagtgggctg acatagaccc agtgccccag 240 aatgatggcc ccagtccagt ggtccagatc atctacagtg aaaagtttag agacgtctat 300 gattacttcc gagctgttct gcagcgcgat gaaagaagcg aacgagcctt taagctcact 360 cgagatgcta ttgagttaaa cgcagccaac tatacggtgt ggcattttcg gagagttctc 420 ttgaggtcgc ttcagaagga tctgcaagaa gaaatgaact acatcatcgc aataattgag 480 gaacagccca aaaactatca agtttggcac cataggagag tattagtgga gtggctgaaa 540 gatccttctc aagagctcga gttcatcgcc gatatcctta atcaggatgc aaagaattac 600 catgcctggc agcatcgaca gtgggtcatt caggagtttc gactttggga taatgagctg 660 cagtatgtgg accagcttct caaagaggat gtgagaaata actctgtgtg gaaccaaaga 720 cacttcgtca tttctaatac cactggctac agtgatcgcg ctgtgttgga gagagaagtc 780 caatatactc tggaaatgat caaattagtg ccacacaatg agagtgcgtg gaactacttg 840 aaagggattt tgcaggaccg tggtctttcc agatacccta atctattaaa ccagttgctt 900 gatttacaac caagtcacag ctccccctac ctaattgcct ttcttgtgga tatctatgaa 960 gacatgctgg aaaaccagtg tgacaacaag gaggacattc ttaataaagc actagagtta 1020 tgtgagattc tagctaaaga aaaggacact ataagaaagg aatattggag atatattgga 1080 cggtccctcc agagtaaaca cagcagagaa agtgacatac cggcgagtgt atag 1134 6 1314 DNA Rattus norvegicus 6 atggcttctt cgagttcctt cacctattat tgtcctccat cttcttcccc tgtttggtca 60 gaaccgctgt atagtctgag acctgagcac gcgcgggagc ggttgcaaga cgactcagtg 120 gaaacagtca cgtccataga acaggccaaa gtagaagaaa agatccagga ggtcttcagt 180 tcttacaagt ttaaccacct cgtaccaagg ctcgttctgc agagggagaa gcacttccat 240 tatctgaaaa gaggccttcg acaactgaca gatgcctatg agtgtctgga tgccagccgc 300 ccctggctct gctactggat cctgcacagc ttggagctcc tcgacgaacc catcccccaa 360 atagtggcta cagatgtgtg tcagttcttg gagctgtgtc agagtccaga cggtggcttt 420 ggagggggcc ctggtcagta cccacacctc gctcccacgt atgcagctgt caacgcgcta 480 tgcatcattg gcacggagga agcctacaac gtcattaaca gagagaagct ccttcagtac 540 ttgtactccc taaagcaacc ggatggctct tttctcatgc acgtcggagg agaggtggat 600 gtaagaagtg cgtactgtgc tgcctcagta gcctctctca ccaacatcat cactcctgac 660 ctcttcgaag gcactgctga atggatagca aggtgccaga actgggaagg cggcattggc 720 ggggtgccag ggatggaagc ccacggtggc tacaccttct gtggcttggc tgcgctggtg 780 atcctcaaga aggaacgttc tttgaacctg aagagcttgc tacaatgggt gacaagccgg 840 cagatgcggt tcgaaggagg atttcagggc cgctgcaaca agctggtgga cggctgctac 900 tccttctggc aggcaggact tctgcccctg ttgcaccggg cactccacgc tcaaggtgac 960 cctgccctca gcatgagcca ctggatgttc catcagcagg cgctgcagga gtacatcctc 1020 atgtgctgcc agtgtccggc tgggggtctc ctggacaaac ctggcaagtc acgtgacttc 1080 taccatactt gctactgcct gagcggcctg tccattgccc agcattttgg aagtggagcc 1140 atgctgcacg atgtggtcat gggtgtgcct gaaaatgttc tgcagcccac tcaccctgtg 1200 tacaacatcg gacctgataa ggtgatccag gccaccacac actttctgca gaagccggtc 1260 ccaggctttg aggaatgcga agatgcggtg acctcagatc ctgccactga ctag 1314 

We claim:
 1. A crystalline complex comprising rat farnesyl protein transferase complexed with α-hydroxy phosphonic acid and a peptide whose amino acid sequence consists of AcCys-Val-Ile-Met(Se) (SEQ ID NO: 1).
 2. The crystalline complex of claim 1 whose structural coordinates are set forth in Table
 2. 3. A crystalline complex comprising rat farnesyl protein transferase complexed with farnesyl diphosphate and an FPT inhibitor selected from the group consisting of SCH66381, SCH66701 and SCH69132.
 4. The crystalline complex of claim 3 whose structural coordinates are set forth in Table
 3. 5. The crystalline complex of claim 3 whose structural coordinates are set forth in Table
 4. 6. The crystalline complex of claim 3 whose structural coordinates are set forth in Table
 5. 7. A crystalline complex comprising rat farnesyl protein transferase which transferase consists of an α-subunit encoded by the nucleotide sequence of SEQ ID NO: 5 and a β-subunit encoded by the nucleotide sequence of SEQ ID NO: 6, complexed with α-hydroxy phosphonic acid and a peptide whose amino acid sequence consists of AcCys-Val-Ile-Met(Se) (SEQ ID NO: 1).
 8. The crystalline complex of claim 7 whose structural coordinates are set forth in Table
 2. 9. A crystalline complex comprising rat farnesyl protein transferase which transferase consists of an α-subunit encoded by the nucleotide sequence of SEQ ID NO: 5 and a β-subunit encoded by the nucleotide sequence of SEQ ID NO: 6, complexed with farnesyl diphosphate and an FPT inhibitor selected from the group consisting of SCH66381, SCH66701 and SCH69132.
 10. The crystalline complex of claim 9 whose structural coordinates are set forth in Table
 3. 11. The crystalline complex of claim 9 whose structural coordinates are set forth in Table
 4. 12. The crystalline complex of claim 9 whose structural coordinates are set forth in Table
 5. 